ID FDHA_DESGI Reviewed; 1012 AA. AC Q934F5; DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot. DT 26-FEB-2008, sequence version 2. DT 10-AUG-2010, entry version 61. DE RecName: Full=Formate dehydrogenase subunit alpha; DE Short=FDH subunit alpha; DE EC=1.2.1.2; DE AltName: Full=Formate dehydrogenase large subunit; DE Flags: Precursor; GN Name=fdhA; OS Desulfovibrio gigas. OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales; OC Desulfovibrionaceae; Desulfovibrio. OX NCBI_TaxID=879; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, COFACTOR, DISULFIDE BOND, RP CALCIUM-BINDING, METAL-BINDING, AND X-RAY CRYSTALLOGRAPHY (1.8 RP ANGSTROMS) IN COMPLEX WITH FDHB. RC STRAIN=ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759; RX PubMed=12220497; DOI=10.1016/S0969-2126(02)00826-2; RA Raaijmakers H., Macieira S.I.M.G., Dias J.M., Teixeira S., RA Bursakov S., Huber R., Moura J.J.G., Moura I., Romao M.J.; RT "Gene sequence and the 1.8 A crystal structure of the tungsten- RT containing formate dehydrogenase from Desulfovibrio gigas."; RL Structure 10:1261-1272(2002). RN [2] RP CHARACTERIZATION. RA Riederer-Henderson M.A., Peck H.D. Jr.; RT "Properties of formate dehydrogenase from Desulfivibrio gigas."; RL Can. J. Microbiol. 32:430-435(1986). RN [3] RP CHARACTERIZATION, AND SUBUNIT. RC STRAIN=ATCC 19364 / DSM 1382 / NCIB 9332 / VKM B-1759; RX PubMed=10587462; DOI=10.1021/bi990069n; RA Almendra M.J., Brondino C.D., Gavel O., Pereira A.S., Tavares P., RA Bursakov S., Duarte R., Caldeira J., Moura J.J.G., Moura I.; RT "Purification and characterization of a tungsten-containing formate RT dehydrogenase from Desulfovibrio gigas."; RL Biochemistry 38:16366-16372(1999). RN [4] RP COFACTOR, AND SUBUNIT. RX PubMed=11372198; DOI=10.1007/s007750100215; RA Raaijmakers H., Teixeira S., Dias J.M., Almendra M.J., Brondino C.D., RA Moura I., Moura J.J.G., Romao M.J.; RT "Tungsten-containing formate dehydrogenase from Desulfovibrio gigas: RT metal identification and preliminary structural data by multi- RT wavelength crystallography."; RL J. Biol. Inorg. Chem. 6:398-404(2001). CC -!- FUNCTION: Alpha chain of the formate dehydrogenase (FDH) catalyze CC the reversible two-electron oxidation of formate to carbon CC dioxide. FDH loses activity in the presence of air, but this CC activity can be restored. The alpha subunit of formate CC dehydrogenase forms the active site. CC -!- CATALYTIC ACTIVITY: Formate + NAD(+) = CO(2) + NADH. CC -!- COFACTOR: Binds 1 4Fe-4S cluster per subunit. CC -!- COFACTOR: Binds 2 molybdopterin guanine dinucleotide (MGD) groups. CC -!- COFACTOR: Binds 1 tungsten ion per subunit. CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC pH dependence: CC Optimum pH is 7.5-8.0; CC Temperature dependence: CC Optimum temperature is 56 degrees Celsius; CC -!- SUBUNIT: Heterodimer of alpha (fdhA) and beta (fdhB) subunits. CC -!- SUBCELLULAR LOCATION: Periplasm. CC -!- PTM: The disulfide bond is likely to be broken in the active form CC of this enzyme. CC -!- PTM: Predicted to be exported by the Tat system. The position of CC the signal peptide cleavage has been experimentally proven. CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing CC oxidoreductase family. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AJ318781; CAC86667.1; -; Genomic_DNA. DR PDB; 1H0H; X-ray; 1.80 A; A/K=36-1012. DR PDBsum; 1H0H; -. DR ProteinModelPortal; Q934F5; -. DR BRENDA; 1.2.1.2; 7582. DR BRENDA; 1.2.2.1; 7582. DR GO; GO:0005737; C:cytoplasm; IEA:InterPro. DR GO; GO:0042597; C:periplasmic space; IEA:UniProtKB-SubCell. DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW. DR GO; GO:0009055; F:electron carrier activity; IEA:InterPro. DR GO; GO:0008863; F:formate dehydrogenase activity; IEA:EC. DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro. DR GO; GO:0045333; P:cellular respiration; IEA:InterPro. DR GO; GO:0022900; P:electron transport chain; IEA:UniProtKB-KW. DR GO; GO:0006810; P:transport; IEA:UniProtKB-KW. DR InterPro; IPR009010; Asp_de-COase-like_fold. DR InterPro; IPR006443; Formate_DH_asu_anaerob. DR InterPro; IPR006657; MoPterin_dinucl-bd_dom. DR InterPro; IPR006656; Mopterin_OxRdtase. DR InterPro; IPR006963; Mopterin_OxRdtase_Fe4S4_dom. DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS. DR InterPro; IPR006311; TAT_signal. DR Gene3D; G3DSA:2.40.40.20; Asp_decarboxylase-like_fold; 1. DR Pfam; PF04879; Molybdop_Fe4S4; 1. DR Pfam; PF00384; Molybdopterin; 1. DR Pfam; PF01568; Molydop_binding; 1. DR SUPFAM; SSF50692; Asp_decarb_fold; 1. DR TIGRFAMs; TIGR01553; formate-DH-alph; 1. DR TIGRFAMs; TIGR01409; TAT_signal_seq; 1. DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1. DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; FALSE_NEG. DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1. DR PROSITE; PS51318; TAT; 1. PE 1: Evidence at protein level; KW 3D-structure; 4Fe-4S; Calcium; Disulfide bond; Electron transport; KW Iron; Iron-sulfur; Metal-binding; Molybdenum; NAD; Oxidoreductase; KW Periplasm; Selenocysteine; Signal; Transport; Tungsten. FT SIGNAL 1 35 Tat-type signal. FT CHAIN 36 1012 Formate dehydrogenase subunit alpha. FT /FTId=PRO_0000019149. FT CA_BIND 394 398 FT METAL 52 52 Iron-sulfur (4Fe-4S). FT METAL 55 55 Iron-sulfur (4Fe-4S). FT METAL 59 59 Iron-sulfur (4Fe-4S). FT METAL 89 89 Iron-sulfur (4Fe-4S). FT METAL 193 193 Tungsten. FT NON_STD 193 193 Selenocysteine. FT DISULFID 852 879 FT TURN 41 44 FT STRAND 45 51 FT STRAND 53 55 FT STRAND 60 65 FT TURN 67 69 FT STRAND 72 77 FT TURN 82 86 FT HELIX 90 93 FT HELIX 95 99 FT STRAND 109 111 FT HELIX 123 141 FT STRAND 142 145 FT STRAND 151 155 FT STRAND 157 161 FT HELIX 168 180 FT HELIX 190 193 FT HELIX 195 205 FT HELIX 215 219 FT STRAND 221 227 FT HELIX 230 233 FT HELIX 237 246 FT STRAND 250 254 FT HELIX 262 264 FT STRAND 266 269 FT HELIX 276 289 FT HELIX 295 301 FT HELIX 303 305 FT STRAND 306 308 FT TURN 324 327 FT HELIX 331 334 FT HELIX 356 364 FT HELIX 369 376 FT HELIX 380 391 FT HELIX 392 394 FT STRAND 400 404 FT HELIX 411 427 FT STRAND 431 433 FT STRAND 437 440 FT HELIX 447 452 FT TURN 461 463 FT HELIX 474 481 FT HELIX 493 496 FT HELIX 497 508 FT HELIX 514 520 FT HELIX 532 540 FT STRAND 546 551 FT HELIX 554 557 FT STRAND 558 560 FT HELIX 561 568 FT STRAND 572 580 FT TURN 583 586 FT HELIX 587 589 FT HELIX 595 597 FT STRAND 601 607 FT HELIX 610 612 FT STRAND 615 618 FT STRAND 623 627 FT HELIX 640 657 FT HELIX 664 668 FT HELIX 671 674 FT HELIX 683 691 FT STRAND 693 696 FT STRAND 698 700 FT STRAND 703 705 FT HELIX 714 716 FT HELIX 728 730 FT STRAND 733 735 FT HELIX 740 742 FT HELIX 750 755 FT STRAND 761 764 FT TURN 765 768 FT HELIX 774 777 FT HELIX 787 789 FT STRAND 791 795 FT TURN 796 799 FT STRAND 800 804 FT TURN 816 818 FT STRAND 826 829 FT STRAND 851 853 FT STRAND 885 890 FT HELIX 900 903 FT HELIX 906 911 FT STRAND 916 919 FT HELIX 921 927 FT STRAND 934 939 FT STRAND 942 950 FT STRAND 957 959 FT STRAND 962 964 FT STRAND 966 971 FT HELIX 985 987 FT STRAND 991 994 FT STRAND 996 1000 FT STRAND 1005 1011 SQ SEQUENCE 1012 AA; 113271 MW; 23CDC4594334D51F CRC64; MLIKRRAFLK LTAAGATLSA FGGLGVDLAP AKAQAATMAL KTVDAKQTTS VCCYCSVGCG LIVHTDKKTN RAINVEGDPD HPINEGSLCA KGASTWQLAE NERRPANPLY RAPGSDQWEE KSWDWMLDTI AERVAKTREA TFVTKNAKGQ VVNRCDGIAS VGSAAMDNEE CWIYQAWLRS LGLFYIEHQA RIUHSATVAA LAESYGRGAM TNHWIDLKNS DVILMMGSNP AENHPISFKW VMRAKDKGAT LIHVDPRYTR TSTKCDLYAP LRSGSDIAFL NGMTKYILEK ELYFKDYVVN YTNASFIVGE GFAFEEGLFA GYNKETRKYD KSKWGFERDE NGNPKRDETL KHPRCVFQIM KKHYERYDLD KISAICGTPK ELILKVYDAY CATGKPDKAG TIMYAMGWTQ HTVGVQNIRA MSINQLLLGN IGVAGGGVNA LRGEANVQGS TDHGLLMHIY PGYLGTARAS IPTYEEYTKK FTPVSKDPQS ANWWSNFPKY SASYIKSMWP DADLNEAYGY LPKGEDGKDY SWLTLFDDMF QGKIKGFFAW GQNPACSGAN SNKTREALTK LDWMVNVNIF DNETGSFWRG PDMDPKKIKT EVFFLPCAVA IEKEGSISNS GRWMQWRYVG PEPRKNAIPD GDLIVELAKR VQKLLAKTPG KLAAPVTKLK TDYWVNDHGH FDPHKIAKLI NGFALKDFKV GDVEYKAGQQ IATFGHLQAD GSTTSGCWIY TGSYTEKGNM AARRDKTQTD MQAKIGLYPG WTWAWPVNRR IIYNRASVDL NGKPYAPEKA VVEWNAAEKK WVGDVPDGPW PPQADKEKGK RAFIMKPEGY AYLYGPGRED GPLPEYYEPM ECPVIEHPFS KTLHNPTALH FATEEKAVCD PRYPFICSTY RVTEHWQTGL MTRNTPWLLE AEPQMFCEMS EELATLRGIK NGDKVILESV RGKLWAKAII TKRIKPFAIQ GQQVHMVGIP WHYGWSFPKN GGDAANILTP SVGDPNTGIP ETKAFMVNVT KA //