ID A0A0D5M972_9GAMM Unreviewed; 988 AA.
AC A0A0D5M972;
DT 27-MAY-2015, integrated into UniProtKB/TrEMBL.
DT 27-MAY-2015, sequence version 1.
DT 27-MAR-2024, entry version 45.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:AJY52904.1};
GN ORFNames=KO116_P100147 {ECO:0000313|EMBL:AJY52904.1};
OS Halomonas sp. KO116.
OG Plasmid unnamed1 {ECO:0000313|EMBL:AJY52904.1,
OG ECO:0000313|Proteomes:UP000028645}.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Halomonadaceae; Halomonas.
OX NCBI_TaxID=1504981 {ECO:0000313|EMBL:AJY52904.1, ECO:0000313|Proteomes:UP000028645};
RN [1] {ECO:0000313|EMBL:AJY52904.1, ECO:0000313|Proteomes:UP000028645}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KO116 {ECO:0000313|EMBL:AJY52904.1,
RC ECO:0000313|Proteomes:UP000028645};
RC PLASMID=Plasmid unnamed1 {ECO:0000313|Proteomes:UP000028645};
RX PubMed=25953187;
RA O'Dell K.B., Woo H.L., Utturkar S., Klingeman D., Brown S.D., Hazen T.C.;
RT "Genome Sequence of Halomonas sp. Strain KO116, an Ionic Liquid-Tolerant
RT Marine Bacterium Isolated from a Lignin-Enriched Seawater Microcosm.";
RL Genome Announc. 3:0-0(2015).
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: Belongs to the complex I 75 kDa subunit family.
CC {ECO:0000256|ARBA:ARBA00005404}.
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DR EMBL; CP011053; AJY52904.1; -; Genomic_DNA.
DR RefSeq; WP_035556006.1; NZ_CP011053.1.
DR AlphaFoldDB; A0A0D5M972; -.
DR KEGG; hak:KO116_P100147; -.
DR eggNOG; COG3383; Bacteria.
DR HOGENOM; CLU_000422_4_0_6; -.
DR OrthoDB; 9810782at2; -.
DR Proteomes; UP000028645; Plasmid unnamed1.
DR GO; GO:1990204; C:oxidoreductase complex; IEA:UniProt.
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:InterPro.
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:UniProt.
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; 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; 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 PIRSF; PIRSF036643; FDH_alpha; 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; 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.
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 Plasmid {ECO:0000313|EMBL:AJY52904.1}.
FT DOMAIN 79..119
FT /note="4Fe-4S His(Cys)3-ligated-type"
FT /evidence="ECO:0000259|PROSITE:PS51839"
FT DOMAIN 139..166
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 182..211
FT /note="4Fe-4S ferredoxin-type"
FT /evidence="ECO:0000259|PROSITE:PS51379"
FT DOMAIN 260..316
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
SQ SEQUENCE 988 AA; 110007 MW; BD9055538DDD5A76 CRC64;
MSQPCTIIFD GEEIRGIADE PLIDFLEGHG IALPSVCYHP SLGAIETCDA CWVEVNGELK
RGCALRTQEG MQISSRDPQA VAARHEGMDR LLSKHELYCT VCENNNGDCS LHNAVVEMDI
PIQRYEFQPK PHAKDTTSPF YTYDPDQCIL CGRCVEACQN IEVNETLSID YASENPRVLW
DGGKEINDSS CVHCGHCVTV CPCNALMENS MDEHAGPLTS MPWSLKRPMI EIVKKIETTI
SAKPITGISE IDSAWRQPGI KRTKTVCTYC GVGCSFEMWT RDRHILKVQP SPDAPANGIS
TCIKGKFAWD FVNSEKRLTT PLIRENGRFR EASWEEALDL VARRLLEVRD THGSNSLGFI
GSSKASNEEA YLTQKIARLI IGTNSVDNSS RYCQNPATKG LFRTVGYGGD AGTIKDIEQA
EVVVLVGSNT AENHPVIASK IKAAQKLRGQ KLIVMDPRKH EMAERADIFL RPNASTDLIW
ASALSRYMFD NHLADLDFLG RWVNNVEEYR RSLEPFTLDF AEFKTGISKQ ELINTAEMIG
RAKNVCLLWA MGITQHSHGS DTSTALSNLL LVTGNYGKPG TGGYPMRGHN NVQGASDFGC
LRNMYPGYDK VTDESARQRW AKGWGVDPSQ LSNEVGEGNF LMVQSADQGD IKAMYVIGEE
TAFSDANTHN VHSAFENLDF MVVQDIFLSR TAEFADVVLP ACPSVEKDGT FVNTERRIQR
FYEVLPPLGD SRPDWRILTD LAARMGHDWG YTHPSQIMQE CASISPMFAG VTYERLEGWK
SLSWPVAADG TDTPLLYTDG FHTEDGKANL FPMEWKEPEE ATDAEYDLSL DNGRILEQFQ
GANQTGRSQG IWDQAPHGFV EVSPELAAER GIKEGTWVRI TSRRGSIDFP ALITDRVAGK
TLFMPIHFGK PGVNALTGEH NDPVVQTPAY KETAVKLEVL DKRTEPPLPS TNYRFGRRTP
NQGVAVEVKW MQEDYRLPPA QQTNPRKM
//
