GenomeNet

Database: UniProt
Entry: A0A0C2JC40_9ACTN
LinkDB: A0A0C2JC40_9ACTN
Original site: A0A0C2JC40_9ACTN 
ID   A0A0C2JC40_9ACTN        Unreviewed;       286 AA.
AC   A0A0C2JC40;
DT   01-APR-2015, integrated into UniProtKB/TrEMBL.
DT   01-APR-2015, sequence version 1.
DT   27-MAR-2024, entry version 40.
DE   SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:KIH96545.1};
GN   ORFNames=LP52_24235 {ECO:0000313|EMBL:KIH96545.1};
OS   Streptomonospora alba.
OC   Bacteria; Actinomycetota; Actinomycetes; Streptosporangiales;
OC   Nocardiopsaceae; Streptomonospora.
OX   NCBI_TaxID=183763 {ECO:0000313|EMBL:KIH96545.1, ECO:0000313|Proteomes:UP000031675};
RN   [1] {ECO:0000313|Proteomes:UP000031675}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=YIM 90003 {ECO:0000313|Proteomes:UP000031675};
RX   PubMed=25601074; DOI=10.1016/j.chembiol.2014.11.017;
RA   Metelev M., Tietz J.I., Melby J.O., Blair P.M., Zhu L., Livnat I.,
RA   Severinov K., Mitchell D.A.;
RT   "Structure, bioactivity, and resistance mechanism of streptomonomicin, an
RT   unusual lasso Peptide from an understudied halophilic actinomycete.";
RL   Chem. Biol. 22:241-250(2015).
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:KIH96545.1}.
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; JROO01000058; KIH96545.1; -; Genomic_DNA.
DR   RefSeq; WP_040276727.1; NZ_JROO01000058.1.
DR   AlphaFoldDB; A0A0C2JC40; -.
DR   STRING; 183763.LP52_24235; -.
DR   OrthoDB; 9793944at2; -.
DR   Proteomes; UP000031675; Unassembled WGS sequence.
DR   GO; GO:0071949; F:FAD binding; IEA:InterPro.
DR   GO; GO:0016491; F:oxidoreductase activity; IEA:InterPro.
DR   Gene3D; 3.30.465.10; -; 1.
DR   Gene3D; 3.30.390.50; CO dehydrogenase flavoprotein, C-terminal domain; 1.
DR   Gene3D; 3.30.43.10; Uridine Diphospho-n-acetylenolpyruvylglucosamine Reductase, domain 2; 1.
DR   InterPro; IPR005107; CO_DH_flav_C.
DR   InterPro; IPR036683; CO_DH_flav_C_dom_sf.
DR   InterPro; IPR016166; FAD-bd_PCMH.
DR   InterPro; IPR036318; FAD-bd_PCMH-like_sf.
DR   InterPro; IPR016167; FAD-bd_PCMH_sub1.
DR   InterPro; IPR016169; FAD-bd_PCMH_sub2.
DR   InterPro; IPR002346; Mopterin_DH_FAD-bd.
DR   PANTHER; PTHR42659:SF1; BLR6160 PROTEIN; 1.
DR   PANTHER; PTHR42659; XANTHINE DEHYDROGENASE SUBUNIT C-RELATED; 1.
DR   Pfam; PF03450; CO_deh_flav_C; 1.
DR   Pfam; PF00941; FAD_binding_5; 1.
DR   SMART; SM01092; CO_deh_flav_C; 1.
DR   SUPFAM; SSF55447; CO dehydrogenase flavoprotein C-terminal domain-like; 1.
DR   SUPFAM; SSF56176; FAD-binding/transporter-associated domain-like; 1.
DR   PROSITE; PS51387; FAD_PCMH; 1.
PE   4: Predicted;
KW   Reference proteome {ECO:0000313|Proteomes:UP000031675}.
FT   DOMAIN          1..169
FT                   /note="FAD-binding PCMH-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51387"
SQ   SEQUENCE   286 AA;  30225 MW;  C61F1B343C8EDA32 CRC64;
     MEFLSPSTFE DALSAKSSAP EAVPIMGGTD VMVELNFDRR RPGALLDLSR VRELAQWGPE
     GPYLRLGAGV PYTEIVERLA ARAPALARAA RTVASPQIRN RGSVGGNLGT ASPAGDCHPP
     LVAQGALVEL ASVRGVRRVP ARAFYLGPGR SAREDDELVS AVLLPAPAGP QQFSKIGTRN
     AMVIAVASFS LVLDAATRTA GTGIGSAGPR PLRSPQAEEF LAAEFDWQGG AEPSQAAARH
     FAELVAAAAE PIGDVRGSAS YRRHALSVMA RRAWYWCAED YRKGAR
//
DBGET integrated database retrieval system