ID D9VZR4_9ACTN Unreviewed; 761 AA.
AC D9VZR4;
DT 05-OCT-2010, integrated into UniProtKB/TrEMBL.
DT 05-OCT-2010, sequence version 1.
DT 27-MAR-2024, entry version 62.
DE SubName: Full=Formate dehydrogenase, alpha subunit {ECO:0000313|EMBL:EFL15674.1};
GN ORFNames=SSNG_02926 {ECO:0000313|EMBL:EFL15674.1};
OS Streptomyces sp. C.
OC Bacteria; Actinomycetota; Actinomycetes; Kitasatosporales;
OC Streptomycetaceae; Streptomyces.
OX NCBI_TaxID=253839 {ECO:0000313|EMBL:EFL15674.1, ECO:0000313|Proteomes:UP000005763};
RN [1] {ECO:0000313|EMBL:EFL15674.1, ECO:0000313|Proteomes:UP000005763}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C {ECO:0000313|EMBL:EFL15674.1,
RC ECO:0000313|Proteomes:UP000005763};
RG The Broad Institute Genome Sequencing Platform;
RG Broad Institute Microbial Sequencing Center;
RA Fischbach M., Godfrey P., Ward D., Young S., Zeng Q., Koehrsen M.,
RA Alvarado L., Berlin A.M., Bochicchio J., Borenstein D., Chapman S.B.,
RA Chen Z., Engels R., Freedman E., Gellesch M., Goldberg J., Griggs A.,
RA Gujja S., Heilman E.R., Heiman D.I., Hepburn T.A., Howarth C., Jen D.,
RA Larson L., Lewis B., Mehta T., Park D., Pearson M., Richards J.,
RA Roberts A., Saif S., Shea T.D., Shenoy N., Sisk P., Stolte C., Sykes S.N.,
RA Thomson T., Walk T., White J., Yandava C., Straight P., Clardy J., Hung D.,
RA Kolter R., Mekalanos J., Walker S., Walsh C.T., Wieland-Brown L.C.,
RA Haas B., Nusbaum C., Birren B.;
RT "Annotation of Streptomyces sp. strain C.";
RL Submitted (FEB-2009) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
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DR EMBL; GG657750; EFL15674.1; -; Genomic_DNA.
DR AlphaFoldDB; D9VZR4; -.
DR STRING; 253839.SSNG_02926; -.
DR eggNOG; COG0243; Bacteria.
DR HOGENOM; CLU_000422_13_4_11; -.
DR Proteomes; UP000005763; Unassembled WGS sequence.
DR GO; GO:0051539; F:4 iron, 4 sulfur cluster binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0043546; F:molybdopterin cofactor binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR CDD; cd00508; MopB_CT_Fdh-Nap-like; 1.
DR Gene3D; 2.40.40.20; -; 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; IPR009010; Asp_de-COase-like_dom_sf.
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 PANTHER; PTHR43105:SF15; FORMATE DEHYDROGENASE H; 1.
DR PANTHER; PTHR43105; RESPIRATORY NITRATE REDUCTASE; 1.
DR Pfam; PF04879; Molybdop_Fe4S4; 1.
DR Pfam; PF00384; Molybdopterin; 1.
DR Pfam; PF01568; Molydop_binding; 1.
DR PIRSF; PIRSF000144; CbbBc; 2.
DR SMART; SM00926; Molybdop_Fe4S4; 1.
DR SUPFAM; SSF50692; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
DR PROSITE; PS00551; MOLYBDOPTERIN_PROK_1; 1.
PE 4: Predicted;
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}.
FT DOMAIN 33..89
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 720..761
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 733..761
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 761 AA; 83398 MW; 4F57CCD1FCB755C5 CRC64;
MPLDPAIAPP GTRNFRDAGG IPADRWHADQ NGETLVPTHC CFCGVQCGMY LRVDNAGKVF
GVEPRNHDIN RMRLCPKGIN AYQQVNHPDR LTAPLMRRSR DEEFKEASWD EALDFTVSEI
RRIQAAHGND AFGLLGGASL YSEKTYLVGK FGRVALKTRH VDYNGRLCMV SAAGANKLAF
GIDRAANPFS DILLTDCLLI AGSNVGECFP VMTQYVWGAR DRGATLIVVD PRETAIARTA
DVHVPIKPGT DSAFFNAVLH VIVDEGLTDE AYLAAHTTGW DEVKKTVQEY PPARSAEICG
IPASQIVQVA RMFAGADKAM AFHARGIEHH SQGVENCLSV INMCVATGNL GKPGAGYGTI
TGQGNGQGGR EHGQKADLLP GGRSIMNEEH RRQICRIWGI DEADLPTAGT SMMEMVWQMQ
RQEIRGLIGI CNNPFVSLPN YGAVKQGYDT LDFHAQFDFF LSETAANAHV VFPVTVWAED
EGVMANTEAR VVKHNKAQEP PAGVRTDTWV MCELARRLGA GDKFDFPGSR EVFEELRIAS
AGTVNDYYGI TYERLEATGG IAWPCPSTEH PGTPRLFEDG RTYHPDGKIH MQVVEWHPPM
DAYTEEFPLS LTTGRTVAHF LSGNQTRRLG ALVEQTPRPW VEVHPSHGFR DGDPVRVVTR
RGSEVFPALV TEAIRPDTVF IPYHWPVPTA ANALTIDALD PRSKIPEYKV CAARIEAAER
VDEVPAPPTA PGCQAYPQTQ VSRTDPLPPT SSQGRGTAER S
//
