ID A0A0S9PXD4_9ACTN Unreviewed; 834 AA.
AC A0A0S9PXD4;
DT 17-FEB-2016, integrated into UniProtKB/TrEMBL.
DT 17-FEB-2016, sequence version 1.
DT 27-MAR-2024, entry version 26.
DE SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:KQP62316.1};
GN ORFNames=ASF47_20150 {ECO:0000313|EMBL:KQP62316.1};
OS Nocardioides sp. Leaf285.
OC Bacteria; Actinomycetota; Actinomycetes; Propionibacteriales;
OC Nocardioidaceae; Nocardioides.
OX NCBI_TaxID=1736322 {ECO:0000313|EMBL:KQP62316.1, ECO:0000313|Proteomes:UP000051495};
RN [1] {ECO:0000313|EMBL:KQP62316.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP62316.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQP62316.1, ECO:0000313|Proteomes:UP000051495}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Leaf285 {ECO:0000313|EMBL:KQP62316.1,
RC ECO:0000313|Proteomes:UP000051495};
RA Schulze-Lefert P.;
RT "Functional overlap of the Arabidopsis leaf and root microbiotas.";
RL Submitted (NOV-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:KQP62316.1}.
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DR EMBL; LMNH01000007; KQP62316.1; -; Genomic_DNA.
DR RefSeq; WP_056865837.1; NZ_LMNH01000007.1.
DR AlphaFoldDB; A0A0S9PXD4; -.
DR Proteomes; UP000051495; Unassembled WGS sequence.
DR GO; GO:0005506; F:iron ion binding; IEA:InterPro.
DR GO; GO:0016491; F:oxidoreductase activity; 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 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 Reference proteome {ECO:0000313|Proteomes:UP000051495}.
FT DOMAIN 29..144
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
FT REGION 1..27
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 808..834
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..27
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 834 AA; 88757 MW; 4D430C5D813C6A18 CRC64;
MTATQERPAE AAKEIGRDRR RKEDQRLITG RTRWTDNIVL PGMVHVAMVR SPFAHARITG
IDKSAAEASP NVVSVITGAD VADVQGALPN AWPITPDQVA PAHPPIAVDR VVFAGEIVAV
VVARSAAEAR DAAELVDVDY DELPAALELK AAAEATPENG GALAHPDLGT NKSAFWKFDS
AEAGTGGNVD EAIAKARADG VVLEREYRQQ RLIPAFMEPR STVVDPTGEQ ITMWSATQIP
HILKFLLAAV TGVSESKIRV IAPDVGGGFG GKLQTTPEEF ITFLLARRLG KPVKYTETRS
ESLMAAHHGR DQWQKLTISA EKDGTVTGLK VELLADLGSH VSLIGGGVPV LGAFMFNAIY
KFPAYQFNCQ TVLTNKTWTD AYRGAGRPEA TFGIERIMDD LAAELGVDPF ELREKNWIKH
EEFPFTTVAG LEYDSGNYEA ATANAKAMFG YDELRAEQKR RRESGDRVQL GIGVSTFTEM
CGLAPSRVLG SLDYGAGGWE HASVRMLPTG KVEVLTGASA HGQGHETAFS QIVADRLGVA
FEDVEILHGD TQVAHKGLDT YGSRSLVVGG EAIVKAADKV IDKAKVIAAH LLEASEDDLE
FSGGRFSVKG TDQGLAMAEV ALATFAAHNL PDGVEPSLDS DATFDPVNFN YPHGTHLCAM
EVDTETGQVT MRKYAACDDI GNIINPLIVE GQLHGGLVQG IAQALWEEAV YDDAGTLVTG
SFVDYLLPTA ADTISFDLDH TTSPATTNTL GTKGVGEAGT IASTPAVVNA VVDALRPLGV
DDVRMPCTPE RVWKAINDAR GGQKAETVGA AAPHFDPSTG MEGTVDRTTG GADA
//