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Database: UniProt
Entry: A0A1H1CVP5_9ACTN
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ID   A0A1H1CVP5_9ACTN        Unreviewed;      1054 AA.
AC   A0A1H1CVP5;
DT   12-APR-2017, integrated into UniProtKB/TrEMBL.
DT   12-APR-2017, sequence version 1.
DT   27-MAR-2024, entry version 27.
DE   SubName: Full=Formate dehydrogenase major subunit {ECO:0000313|EMBL:SDQ68325.1};
GN   ORFNames=SAMN04489765_1403 {ECO:0000313|EMBL:SDQ68325.1};
OS   Tsukamurella pulmonis.
OC   Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Tsukamurellaceae;
OC   Tsukamurella.
OX   NCBI_TaxID=47312 {ECO:0000313|EMBL:SDQ68325.1, ECO:0000313|Proteomes:UP000183053};
RN   [1] {ECO:0000313|Proteomes:UP000183053}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=DSM 44142 {ECO:0000313|Proteomes:UP000183053};
RA   Varghese N.;
RL   Submitted (OCT-2016) 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}.
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DR   EMBL; FNLF01000002; SDQ68325.1; -; Genomic_DNA.
DR   STRING; 47312.SAMN04489765_1403; -.
DR   Proteomes; UP000183053; Unassembled WGS sequence.
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:InterPro.
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:0045333; P:cellular respiration; IEA:InterPro.
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; 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   NCBIfam; TIGR01553; formate-DH-alph; 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   Selenium {ECO:0000313|EMBL:SDQ68325.1};
KW   Selenocysteine {ECO:0000313|EMBL:SDQ68325.1}.
FT   DOMAIN          43..99
FT                   /note="4Fe-4S Mo/W bis-MGD-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51669"
FT   NON_STD         189
FT                   /note="Selenocysteine"
FT                   /evidence="ECO:0000313|EMBL:SDQ68325.1"
SQ   SEQUENCE   1054 AA;  115749 MW;  43A656E77589C4EB CRC64;
     MTRFSPLEWP VLRQLRSGDV FGRGPAVESP RTRALEPRTK TADRVVQSVC PFCAVGCGQK
     VYVKDEKVIQ IEGDPDSPIS RGRLCPKGSS SEQLVNNPLR QTKIRYRAPY ATEWQDLDRD
     TAIEMIADRF VEARRHGWQD FDEHGRPLRR TMGIASLGGA TLDNEENYLI KKLFTAAGAI
     QIENQARIUH SATVPGLGAS FGRGGATQSL QDMANADCIV LMGGNMAEAH PVGFQWVAEA
     KARGARVIHV DPRFTRTSAV ADRHVPIRAG SDIVLLGGLI NHVLATDAYF HDYVVAYTNA
     AEMVGEDFRD TEDLDGLFSG FDPETGKYDQ STWQYAPGRD ETLQDPRTVF QVVRRHYARY
     TPEVVADMCG ISPAEFAYLA ESITSNSGRE RTTCFGYATG WTQHTMGAQF IRTAAILQLL
     LGNVGRPGSG IMALRGHASI QGSTDIPTLF NLLPGYLPMP SVGRHDTLAD YLAAVRPETG
     KGYWQYADAY MISLLKAWYG DAATAENDFA YDYLPKLNGP AGTYQTAVDM LDGKVDGYFV
     LGQNPAVGSA NGRQQRMGMA KLKWLVVRDL NMIESATWWK DGPEIASGEL RTEEIGTEVF
     FMPAATHVEK AGSFTQTQRM LQWRHQAVQP PGQAQSELDF FYELGLRIRE RLAGSTDERD
     RPLLDLTWDY PMDEHGNPDP EAVLSEINGR FVSGPDAGRN LTTYTELKAD GSTIAGCWIY
     TGVYADGANR AARRVPQGGG GITQSEWGWV WPADRRMLYN RASADPQGRP WSERKKYLWW
     DEAAGRWTGA DVPDFPATLA PGTVPEPGAT GAEALAGDDP FIMQSDGKGW LFAPTGLVDG
     PLPTHYEAQE SPVRNAIHPQ QQAPARVLFP REDNLDAPSA GDPGADVYPY VFTTYRLTEH
     HTAGGMSRWS PYLAELQPEM FCEVSPGLAA ECGLENEGWA TIISPRAAIE CRVLVTERMR
     PLTVGGRTVH QVGLPYHWGV GSDAVVTGDA ANDLIGVTLD PNTQIQESKV GSCTVIAGRR
     PRGAALEDLV QSYRDRAGVT VDTDNVRLTP PREA
//
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