ID A0A2A9EQH8_9MICO Unreviewed; 1096 AA.
AC A0A2A9EQH8;
DT 20-DEC-2017, integrated into UniProtKB/TrEMBL.
DT 20-DEC-2017, sequence version 1.
DT 27-MAR-2024, entry version 24.
DE SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:PFG40459.1};
GN ORFNames=ATJ97_2989 {ECO:0000313|EMBL:PFG40459.1};
OS Georgenia soli.
OC Bacteria; Actinomycetota; Actinomycetes; Micrococcales; Bogoriellaceae;
OC Georgenia.
OX NCBI_TaxID=638953 {ECO:0000313|EMBL:PFG40459.1, ECO:0000313|Proteomes:UP000222106};
RN [1] {ECO:0000313|EMBL:PFG40459.1, ECO:0000313|Proteomes:UP000222106}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 21838 {ECO:0000313|EMBL:PFG40459.1,
RC ECO:0000313|Proteomes:UP000222106};
RA Klenk H.-P.;
RT "Sequencing the genomes of 1000 actinobacteria strains.";
RL Submitted (OCT-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=[4Fe-4S] cluster; Xref=ChEBI:CHEBI:49883;
CC Evidence={ECO:0000256|ARBA:ARBA00001966};
CC -!- SIMILARITY: Belongs to the prokaryotic molybdopterin-containing
CC oxidoreductase family. {ECO:0000256|ARBA:ARBA00010312}.
CC -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:PFG40459.1}.
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; PDJI01000004; PFG40459.1; -; Genomic_DNA.
DR Proteomes; UP000222106; Unassembled WGS sequence.
DR GO; GO:0051536; F:iron-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:UniProtKB-KW.
DR CDD; cd02792; MopB_CT_Formate-Dh-Na-like; 1.
DR Gene3D; 2.40.40.20; -; 1.
DR Gene3D; 3.30.200.210; -; 1.
DR Gene3D; 3.40.50.740; -; 1.
DR Gene3D; 3.40.228.10; Dimethylsulfoxide Reductase, domain 2; 2.
DR InterPro; IPR009010; Asp_de-COase-like_dom_sf.
DR InterPro; IPR048158; Formate_DH_Act.
DR InterPro; IPR006657; MoPterin_dinucl-bd_dom.
DR InterPro; IPR006656; Mopterin_OxRdtase.
DR InterPro; IPR006963; Mopterin_OxRdtase_4Fe-4S_dom.
DR NCBIfam; NF041513; formate_DH_Act; 1.
DR PANTHER; PTHR43598:SF1; FORMATE DEHYDROGENASE, NITRATE-INDUCIBLE, MAJOR SUBUNIT; 1.
DR PANTHER; PTHR43598; TUNGSTEN-CONTAINING FORMYLMETHANOFURAN DEHYDROGENASE 2 SUBUNIT B; 1.
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; ADC-like; 1.
DR SUPFAM; SSF53706; Formate dehydrogenase/DMSO reductase, domains 1-3; 1.
DR PROSITE; PS51669; 4FE4S_MOW_BIS_MGD; 1.
PE 3: Inferred from homology;
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 Oxidoreductase {ECO:0000256|ARBA:ARBA00023002};
KW Reference proteome {ECO:0000313|Proteomes:UP000222106};
KW Selenium {ECO:0000313|EMBL:PFG40459.1};
KW Selenocysteine {ECO:0000313|EMBL:PFG40459.1}.
FT DOMAIN 43..99
FT /note="4Fe-4S Mo/W bis-MGD-type"
FT /evidence="ECO:0000259|PROSITE:PS51669"
FT REGION 337..378
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 822..856
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1075..1096
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 338..360
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 822..836
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT NON_STD 189
FT /note="Selenocysteine"
FT /evidence="ECO:0000313|EMBL:PFG40459.1"
SQ SEQUENCE 1096 AA; 122124 MW; F28051ACFE7679A3 CRC64;
MVGKVFLDWP VVRQLTGADL LGRGRAVRSA RTDALTARTT TADRVARSVC PYCAVGCGQR
VYVKDEQVVQ IEGDPDSPIS RGRLCPKGSA SKSLVTNPAR LSTVRYRRPY GTEWEDLPLD
VAMEMIADRV VKAREQTWQD LDERGRKVRR TLGIASLGGA TLDNEENYLI KKLFTALGAL
QIENQARIUH SSTVPGLGTS FGRGGATGFQ QDLANADCIV IQGSNMAEAH PVGFQWVMEA
KRRGARVIHV DPRFTRTSAL ADQFVPLRAG TDIVFLGAII NYVLSNELDF REYVLAYTNA
ATILDERFTD TEDLDGLFSG FDPERRSYDT DSWQYAEAAP EEGREEHEAD RERASARPME
HETHGLQVQG HPPRDETLQD PRTVYQVLRR HFSRYTPEMV EEACGVPRED FLKVAEAWVA
NSGRERTTAL VYSVGWTQHS VGAQYIRTGA ILQLLLGNMG RPGGGILALR GHASIQGSTD
IPTLFNLLPG YLPMPHADEH QDLQTWIDSM RQPGAKGFWK QADAYAVSLL KAYWGEAATA
ENDFAFDYLP RMTGDHGTYR TVLDMIDGKV KGYFLLGQNP AVGSAHGRAQ RLGMANLDWL
VVRDLYEIES ATFWKDGPEV ATGEIVPEEC RTEVFLMPAA SHVEKEGTFT QTQRMLQWRE
KAVDPTGDRR SELWFFYHLG RLVRERLAGS TLERDRPVLD LAWDYPTHGP TAEPSAEAVL
REINGYEVAT GRELSTFTEM RADGSTVGGC WIYTGVYADG VNQAARRRPG SEQSWVAPEW
GWAWPANRRI LYNRASADPQ GRPWSERKAY VWWDEDAGEW TGHDVPDFER TKPPSYRPPE
GADGTEGLAG DDPFIMQGDG KGALYVPTGL LDGPLPTHYE PVESPFRNPL YGQQANPTRV
EYRRADNPVH PSPAPEQADV FPYVYTTSRL TEHHTAGGMS RTLEYLSELQ PEMFVEVSPQ
LAAERGLEHM GWCHVVTARS AVEGRVMVTD RLRPLRVEGR TIHQVWLPYH WGSGGLVTGD
SANDLFGISL EPNVLIQETK AGTCDVRPGR RPTGTALLDY VAGYRRRAGI LDGDGGDIVT
ARQPDTRQTE EGDHGR
//
