ID A0A0N0D8V7_9RHOB Unreviewed; 808 AA.
AC A0A0N0D8V7;
DT 09-DEC-2015, integrated into UniProtKB/TrEMBL.
DT 09-DEC-2015, sequence version 1.
DT 27-MAR-2024, entry version 20.
DE SubName: Full=Carbon monoxide dehydrogenase large chain {ECO:0000313|EMBL:KPA21618.1};
DE EC=1.2.99.2 {ECO:0000313|EMBL:KPA21618.1};
GN Name=coxL {ECO:0000313|EMBL:KPA21618.1};
GN ORFNames=shim_23250 {ECO:0000313|EMBL:KPA21618.1};
OS Shimia sp. SK013.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae.
OX NCBI_TaxID=1389006 {ECO:0000313|EMBL:KPA21618.1, ECO:0000313|Proteomes:UP000037951};
RN [1] {ECO:0000313|EMBL:KPA21618.1, ECO:0000313|Proteomes:UP000037951}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SK013 {ECO:0000313|EMBL:KPA21618.1,
RC ECO:0000313|Proteomes:UP000037951};
RA Voget S., Kanukollu S., Daniel R., Engelen B.;
RT "Genome Sequence of Shimia sp. SK013.";
RL Submitted (MAR-2015) to the EMBL/GenBank/DDBJ databases.
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:KPA21618.1}.
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; LAJH01000012; KPA21618.1; -; Genomic_DNA.
DR RefSeq; WP_054002761.1; NZ_LAJH01000012.1.
DR AlphaFoldDB; A0A0N0D8V7; -.
DR STRING; 1389006.shim_23250; -.
DR PATRIC; fig|1389006.3.peg.2393; -.
DR OrthoDB; 9758509at2; -.
DR Proteomes; UP000037951; Unassembled WGS sequence.
DR GO; GO:0018492; F:carbon-monoxide dehydrogenase (acceptor) activity; IEA:InterPro.
DR GO; GO:0005507; F:copper ion binding; IEA:InterPro.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0030151; F:molybdenum ion binding; IEA:InterPro.
DR Gene3D; 3.90.1170.50; Aldehyde oxidase/xanthine dehydrogenase, a/b hammerhead; 1.
DR Gene3D; 3.30.365.10; Aldehyde oxidase/xanthine dehydrogenase, molybdopterin binding domain; 4.
DR InterPro; IPR000674; Ald_Oxase/Xan_DH_a/b.
DR InterPro; IPR036856; Ald_Oxase/Xan_DH_a/b_sf.
DR InterPro; IPR016208; Ald_Oxase/xanthine_DH-like.
DR InterPro; IPR008274; AldOxase/xan_DH_MoCoBD1.
DR InterPro; IPR046867; AldOxase/xan_DH_MoCoBD2.
DR InterPro; IPR037165; AldOxase/xan_DH_Mopterin-bd_sf.
DR InterPro; IPR012780; CO_Mo_DH_lsu.
DR NCBIfam; TIGR02416; CO_dehy_Mo_lg; 1.
DR PANTHER; PTHR11908:SF164; DEHYDROGENASE, MOLYBDENUM BINDING SUBUNIT-RELATED; 1.
DR PANTHER; PTHR11908; XANTHINE DEHYDROGENASE; 1.
DR Pfam; PF01315; Ald_Xan_dh_C; 1.
DR Pfam; PF02738; MoCoBD_1; 1.
DR Pfam; PF20256; MoCoBD_2; 1.
DR SMART; SM01008; Ald_Xan_dh_C; 1.
DR SUPFAM; SSF54665; CO dehydrogenase molybdoprotein N-domain-like; 1.
DR SUPFAM; SSF56003; Molybdenum cofactor-binding domain; 1.
PE 4: Predicted;
KW Oxidoreductase {ECO:0000313|EMBL:KPA21618.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000037951}.
FT DOMAIN 31..140
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 808 AA; 87749 MW; BB7436CF46230202 CRC64;
MNKELTREER TDALGGMGCK RKRVEDARFT QGKGNYVDDI QLPGMLQGDF VRSPYAHARV
KSIDSSAAMA LDGVIAVLTA EDLAPLGLHW MPTLAGDKQM VLADGKVLFQ GQEVAFVVAK
DRYIAADAVE LVEVDYEELP VLTDPFAAME SDVVLREDLL GDGGSLPDGA HGPRKHPNHI
FTWEVGEKDA TEQVLDEADV VAEETVYYHR THPCPLETCG CVASMDKVNG KLTLHGTFQA
PHAIRTVVSL ISGIEEHNIR VISPDIGGGF GNKVGAYPGY VCSVVASIVT GVPVKWVEDR
MENLMTTAFA RDYHMTGKIS ATKEGKITGL HCHVTADHGG FDACADPTKF PAGFMNICTG
SYDIPTAYLA VDGVYTNKAP GGVSYRCSFR VTEAAYFIER MVEVLAIELS MDAAELRRIN
FIKKEQFPYQ SALGWEYDSG DYHTAWDKAL KAVDYDGLRA EQAQRVEEFK AGKTRKLMGV
GLTHFTEIVG AGPVKNCDIL GLGMFDSCEI RIHPTGSAIA RLGTISQGQG HATTFAQILA
TEIGLPADSI TIEEGDTDTA PYGLGTYGSR STPVAGAATA MAGRKIRAKA QMIAAYLLEV
HDDDVEFDVD RFVIKGAPEK FKTMKEIAFA AYNQAIPGIE PGLEAVSYYD PPNMTYPFGA
YVCVMDIDVD TGVTDIRRFY ALDDCGTRIN PMIIEGQVHG GLTEALAVAL GQEIAYDDMG
NVKTGTLMDF FLPTAWEVPN YETDHTVTPS PHHPIGAKGV GESPHVGGVP CFSNAVNDAF
RAFGLRHTNM PHDHWRIWKT ANDLGLHG
//