ID Q5V639_HALMA Unreviewed; 1103 AA.
AC Q5V639;
DT 07-DEC-2004, integrated into UniProtKB/TrEMBL.
DT 07-DEC-2004, sequence version 1.
DT 27-MAR-2024, entry version 112.
DE RecName: Full=formate dehydrogenase {ECO:0000256|ARBA:ARBA00013128};
DE EC=1.17.1.9 {ECO:0000256|ARBA:ARBA00013128};
GN Name=fdhG {ECO:0000313|EMBL:AAV45013.1};
GN OrderedLocusNames=pNG7318 {ECO:0000313|EMBL:AAV45013.1};
GN ORFNames=E6P14_03640 {ECO:0000313|EMBL:QCP89982.1};
OS Haloarcula marismortui (strain ATCC 43049 / DSM 3752 / JCM 8966 / VKM
OS B-1809) (Halobacterium marismortui).
OG Plasmid pHMA411 {ECO:0000313|EMBL:QCP89982.1},
OG Plasmid pNG700 {ECO:0000313|EMBL:AAV45013.1,
OG ECO:0000313|Proteomes:UP000001169}, and
OG Plasmid phma411 {ECO:0000313|Proteomes:UP000298722}.
OC Archaea; Euryarchaeota; Stenosarchaea group; Halobacteria; Halobacteriales;
OC Haloarculaceae; Haloarcula.
OX NCBI_TaxID=272569 {ECO:0000313|EMBL:AAV45013.1, ECO:0000313|Proteomes:UP000001169};
RN [1] {ECO:0000313|EMBL:AAV45013.1, ECO:0000313|Proteomes:UP000001169}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:AAV45013.1}, and ATCC 43049 / DSM
RC 3752 / JCM 8966 / VKM B-1809 {ECO:0000313|Proteomes:UP000001169};
RC PLASMID=Plasmid pNG700 {ECO:0000313|Proteomes:UP000001169}, and pNG700
RC {ECO:0000313|EMBL:AAV45013.1};
RX PubMed=15520287; DOI=10.1101/gr.2700304;
RA Baliga N.S., Bonneau R., Facciotti M.T., Pan M., Glusman G., Deutsch E.W.,
RA Shannon P., Chiu Y., Weng R.S., Gan R.R., Hung P., Date S.V., Marcotte E.,
RA Hood L., Ng W.V.;
RT "Genome sequence of Haloarcula marismortui: a halophilic archaeon from the
RT Dead Sea.";
RL Genome Res. 14:2221-2234(2004).
RN [2] {ECO:0000313|EMBL:QCP89982.1, ECO:0000313|Proteomes:UP000298722}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 43049 {ECO:0000313|EMBL:QCP89982.1,
RC ECO:0000313|Proteomes:UP000298722};
RC PLASMID=pHMA411 {ECO:0000313|EMBL:QCP89982.1}, and phma411
RC {ECO:0000313|Proteomes:UP000298722};
RA DasSarma S., DasSarma P., DasSarma S., Fomenkov A., Vincze T., Anton B.P.,
RA Roberts R.J.;
RT "Methylomes of two halophilic Archaea, Haloarcula marismortui and Haloferax
RT mediterranei.";
RL Submitted (APR-2019) to the EMBL/GenBank/DDBJ databases.
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;
CC Evidence={ECO:0000256|ARBA:ARBA00000455};
CC -!- COFACTOR:
CC Name=Mo-bis(molybdopterin guanine dinucleotide);
CC Xref=ChEBI:CHEBI:60539; Evidence={ECO:0000256|ARBA:ARBA00001942};
CC -!- COFACTOR:
CC Name=[2Fe-2S] cluster; Xref=ChEBI:CHEBI:190135;
CC Evidence={ECO:0000256|ARBA:ARBA00034078};
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: In the C-terminal section; belongs to the prokaryotic
CC molybdopterin-containing oxidoreductase family.
CC {ECO:0000256|ARBA:ARBA00007023}.
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DR EMBL; AY596296; AAV45013.1; -; Genomic_DNA.
DR EMBL; CP039137; QCP89982.1; -; Genomic_DNA.
DR RefSeq; WP_011222715.1; NZ_CP039137.1.
DR AlphaFoldDB; Q5V639; -.
DR EnsemblBacteria; AAV45013; AAV45013; pNG7318.
DR GeneID; 40151217; -.
DR KEGG; hma:pNG7318; -.
DR PATRIC; fig|272569.17.peg.745; -.
DR HOGENOM; CLU_000422_2_2_2; -.
DR Proteomes; UP000001169; Plasmid pNG700.
DR Proteomes; UP000298722; Plasmid phma411.
DR GO; GO:0051537; F:2 iron, 2 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
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:0015942; P:formate metabolic process; IEA:InterPro.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR CDD; cd02753; MopB_Formate-Dh-H; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.10.20.740; -; 1.
DR Gene3D; 3.30.70.20; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 2.20.25.90; ADC-like domains; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 1.
DR InterPro; IPR036010; 2Fe-2S_ferredoxin-like_sf.
DR InterPro; IPR001041; 2Fe-2S_ferredoxin-type.
DR InterPro; IPR017896; 4Fe4S_Fe-S-bd.
DR InterPro; IPR017900; 4Fe4S_Fe_S_CS.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR041924; Formate_Dh-H_N.
DR InterPro; IPR006478; Formate_DH_asu.
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; IPR019574; NADH_UbQ_OxRdtase_Gsu_4Fe4S-bd.
DR NCBIfam; TIGR01591; Fdh-alpha; 1.
DR PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF13510; Fer2_4; 1.
DR Pfam; PF12838; Fer4_7; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR Pfam; PF10588; NADH-G_4Fe-4S_3; 1.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SMART; SM00929; NADH-G_4Fe-4S_3; 1.
DR SUPFAM; SSF54292; 2Fe-2S ferredoxin-like; 1.
DR SUPFAM; SSF54862; 4Fe-4S ferredoxins; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51085; 2FE2S_FER_2; 1.
DR PROSITE; PS00198; 4FE4S_FER_1; 1.
DR PROSITE; PS51379; 4FE4S_FER_2; 2.
DR PROSITE; PS51839; 4FE4S_HC3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
DR PROSITE; PS00490; MOLYBDOPTERIN_PROK_2; 1.
DR PROSITE; PS00932; MOLYBDOPTERIN_PROK_3; 1.
PE 3: Inferred from homology;
KW 2Fe-2S {ECO:0000256|ARBA:ARBA00022714};
KW 4Fe-4S {ECO:0000256|ARBA:ARBA00022485};
KW Iron {ECO:0000256|ARBA:ARBA00023004};
KW Iron-sulfur {ECO:0000256|ARBA:ARBA00023014};
KW Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW NAD {ECO:0000256|ARBA:ARBA00023027}; Plasmid {ECO:0000313|EMBL:AAV45013.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000001169};
KW Repeat {ECO:0000256|ARBA:ARBA00022737}.
FT DOMAIN 42..142
FT /note="2Fe-2S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51085"
FT DOMAIN 142..181
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 204..223
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 248..277
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 388..447
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 1..47
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 302..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1081..1103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 23..44
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1103 AA; 120136 MW; F1B6C6672CB3C081 CRC64;
MSTDKSIPRV PDLHDPQPET PVTHEFETGT ANDPDVGTDT DDPTTLTVDG ERVTVAPGST
IIDALQDLDD DIVSVDPGAE GVEDDADVPA LCYYDRDGDC SDEVGPRSEC RTCMVETEEH
GLVPSCSFPA EDGLSVSTDT PDAEEARSVN LDLVLSNHNL RCTTCNGNGR CELQDAAISE
GVDHPRYGVF DERDQYEPID DTSSFIQIDR NKCILCNRCV DACNDVQVEG VLRIEGHGED
TRIGFQSDAE TMHDSECVSC GHCATVCPTG SLTEKGIDGA ATLPLPGFTQ RNSIGKVIEH
EDAETIDDTT APNRGFEPGD PRAAKSKQGL AKFASQAKRR AGDIAKDYGK KAFLAGEHTA
ESIAANTMPE GRLFDIADIV SDYRLSKIDK EETTCGFCAV GCRFEMWGKD GDSLGVVPVD
DPDDAPANNF STCVKGKFGH EFANSEQRVT EPLIRNDDGE LEPTTWDEAL EYVAERFTEI
QDAHGIDSLG CLASSKGSNE EAYLVQKFAR QVLGTKNIDN CARLCHSSTV AALQQTLGYG
AMTNRINEDI GEADAYLISG SNTTESHPVL ATRIKQNVRD GADLVVFDPR KVGIAEHADQ
YTRTNPGYDV AWLNGLIRYI IEHDLHDEAF IERNTKNFEE VREKVQAFTP EKVKELAGVS
PEELASAAET LAEADTVVFG WAMGMTQQSH GTENLIAMAD LALVLGQVGK PGAGLSPFRG
QNNVQGGGGD MGTLPGSLPG YQNPADDEVG EKFADAWGER PPKEPGLKVP EMLAEAHAGN
LRGMYVVGEN PALSEPDIQH AAEALEDLEF LVVQDIFMTE TAEYADVVLP AATSPEKHGT
FTNTERRIQR VRPTSEPPGK ARQDWEITQA LARRLGYDWD YDHPREVMDE INSLAPIYGG
VTYDRLESGE EHGLQWPCWD EDHDGTPYLY DYDEGNFNFE DGKARFVPAD GGHPGEIPDE
EFPLTLTSGR VLYHWHTGQI TRRVEGLMSH VGESFVEVHP ETAEKLGIAD GEYVRVESRR
GDIVVKAQVT DRVGPGTLFI PMHFAAGAVN KLTGETFDPT AGIPEYKVSS VRVEVLGPET
DETVLRTPDA GGKQIRKRGT GDD
//
