FDHA_MEGGA
ID FDHA_MEGGA Reviewed; 1012 AA.
AC Q934F5;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=Formate dehydrogenase subunit alpha;
DE Short=FDH subunit alpha;
DE EC=1.17.1.9;
DE AltName: Full=Formate dehydrogenase large subunit;
DE Flags: Precursor;
GN Name=fdhA {ECO:0000303|PubMed:12220497};
OS Megalodesulfovibrio gigas (Desulfovibrio gigas).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Desulfovibrionales;
OC Desulfovibrionaceae; Megalodesulfovibrio.
OX NCBI_TaxID=879 {ECO:0000312|EMBL:CAC86667.1};
RN [1] {ECO:0007744|PDB:1H0H}
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA], SUBUNIT, COFACTOR, DISULFIDE BOND,
RP CALCIUM-BINDING, METAL-BINDING, AND X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS)
RP 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., Bursakov S.,
RA Huber R., Moura J.J.G., Moura I., Romao M.J.;
RT "Gene sequence and the 1.8 A crystal structure of the tungsten-containing
RT formate dehydrogenase from Desulfovibrio gigas.";
RL Structure 10:1261-1272(2002).
RN [2] {ECO:0000305}
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] {ECO:0000305}
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] {ECO:0000305}
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: metal
RT identification and preliminary structural data by multi-wavelength
RT crystallography.";
RL J. Biol. Inorg. Chem. 6:398-404(2001).
CC -!- FUNCTION: Alpha chain of the formate dehydrogenase (FDH) catalyze the
CC reversible two-electron oxidation of formate to carbon dioxide. FDH
CC loses activity in the presence of air, but this activity can be
CC restored. The alpha subunit of formate dehydrogenase forms the active
CC site.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=formate + NAD(+) = CO2 + NADH; Xref=Rhea:RHEA:15985,
CC ChEBI:CHEBI:15740, ChEBI:CHEBI:16526, ChEBI:CHEBI:57540,
CC ChEBI:CHEBI:57945; EC=1.17.1.9; Evidence={ECO:0000305};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Note=Binds 1 [4Fe-4S] cluster per subunit.;
CC -!- COFACTOR:
CC Name=W-bis(molybdopterin guanine dinucleotide); Xref=ChEBI:CHEBI:60537;
CC Note=Binds 1 W-bis(molybdopterin guanine dinucleotide) (W-bis-MGD)
CC cofactor 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 {ECO:0000269|PubMed:10587462, ECO:0000269|PubMed:11372198,
CC ECO:0000269|PubMed:12220497}.
CC -!- SUBCELLULAR LOCATION: Periplasm.
CC -!- PTM: The disulfide bond is likely to be broken in the active form of
CC this enzyme. {ECO:0000303|PubMed:12220497}.
CC -!- PTM: Predicted to be exported by the Tat system. The position of the
CC signal peptide cleavage has been experimentally proven.
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) 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 SMR; Q934F5; -.
DR OMA; KWDGAKW; -.
DR EvolutionaryTrace; Q934F5; -.
DR GO; GO:0009326; C:formate dehydrogenase complex; IEA:UniProtKB-EC.
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 transfer activity; IEA:InterPro.
DR GO; GO:0047111; F:formate dehydrogenase (cytochrome-c-553) activity; IEA:InterPro.
DR GO; GO:0008863; F:formate dehydrogenase (NAD+) activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0045333; P:cellular respiration; IEA:InterPro.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR006443; Formate-DH-alph_fdnG.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR InterPro; IPR006655; Mopterin_OxRdtase_prok_CS.
DR InterPro; IPR027467; MopterinOxRdtase_cofactor_BS.
DR InterPro; IPR006311; TAT_signal.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; SSF50692; 1.
DR TIGRFAMs; TIGR01553; formate-DH-alph; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
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; Iron;
KW Iron-sulfur; Metal-binding; NAD; Oxidoreductase; Periplasm; Selenocysteine;
KW Signal; Transport; Tungsten.
FT SIGNAL 1..35
FT /note="Tat-type signal"
FT CHAIN 36..1012
FT /note="Formate dehydrogenase subunit alpha"
FT /id="PRO_0000019149"
FT DOMAIN 45..103
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004"
FT BINDING 52
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:12220497, ECO:0007744|PDB:1H0H"
FT BINDING 55
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:12220497, ECO:0007744|PDB:1H0H"
FT BINDING 59
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:12220497, ECO:0007744|PDB:1H0H"
FT BINDING 89
FT /ligand="[4Fe-4S] cluster"
FT /ligand_id="ChEBI:CHEBI:49883"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01004,
FT ECO:0000269|PubMed:12220497, ECO:0007744|PDB:1H0H"
FT BINDING 193
FT /ligand="W-bis(molybdopterin guanine dinucleotide)"
FT /ligand_id="ChEBI:CHEBI:60537"
FT /ligand_part="W"
FT /ligand_part_id="ChEBI:CHEBI:27998"
FT /evidence="ECO:0000269|PubMed:12220497"
FT BINDING 393
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1H0H"
FT BINDING 395
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1H0H"
FT BINDING 398
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1H0H"
FT BINDING 428
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1H0H"
FT BINDING 430
FT /ligand="Ca(2+)"
FT /ligand_id="ChEBI:CHEBI:29108"
FT /evidence="ECO:0007744|PDB:1H0H"
FT NON_STD 193
FT /note="Selenocysteine"
FT /evidence="ECO:0000269|PubMed:12220497"
FT DISULFID 852..879
FT /evidence="ECO:0000269|PubMed:12220497"
FT TURN 41..44
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 45..51
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 53..55
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 60..65
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 67..69
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 72..77
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 82..86
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 90..93
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 95..99
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 109..111
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 123..141
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 142..145
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 151..155
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 157..161
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 168..180
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 190..193
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 195..205
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 215..219
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 221..227
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 230..233
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 237..246
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 250..254
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 262..264
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 266..269
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 276..289
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 295..301
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 303..305
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 306..308
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 324..327
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 331..334
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 356..364
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 369..376
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 380..391
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 392..394
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 400..404
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 411..427
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 431..433
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 437..440
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 447..452
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 461..463
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 474..481
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 493..496
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 497..508
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 514..520
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 532..540
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 546..551
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 554..557
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 558..560
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 561..568
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 572..580
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 583..586
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 587..589
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 595..597
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 601..607
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 610..612
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 615..618
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 623..627
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 640..657
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 664..668
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 671..674
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 683..691
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 693..696
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 698..700
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 703..705
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 714..716
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 728..730
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 733..735
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 740..742
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 750..755
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 761..764
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 765..768
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 774..777
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 787..789
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 791..795
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 796..799
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 800..804
FT /evidence="ECO:0007829|PDB:1H0H"
FT TURN 816..818
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 826..829
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 851..853
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 885..890
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 900..903
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 906..911
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 916..919
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 921..927
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 934..939
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 942..950
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 957..959
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 962..964
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 966..971
FT /evidence="ECO:0007829|PDB:1H0H"
FT HELIX 985..987
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 991..994
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 996..1000
FT /evidence="ECO:0007829|PDB:1H0H"
FT STRAND 1005..1011
FT /evidence="ECO:0007829|PDB:1H0H"
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
