ID A0A0Q6Z528_9BRAD Unreviewed; 791 AA.
AC A0A0Q6Z528;
DT 20-JAN-2016, integrated into UniProtKB/TrEMBL.
DT 20-JAN-2016, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Carbon monoxide dehydrogenase {ECO:0000313|EMBL:KQW23317.1};
GN ORFNames=ASC80_08580 {ECO:0000313|EMBL:KQW23317.1};
OS Afipia sp. Root123D2.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Hyphomicrobiales;
OC Nitrobacteraceae; Afipia.
OX NCBI_TaxID=1736436 {ECO:0000313|EMBL:KQW23317.1, ECO:0000313|Proteomes:UP000051348};
RN [1] {ECO:0000313|EMBL:KQW23317.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW23317.1,
RC ECO:0000313|Proteomes:UP000051348};
RA Gilbert D.G.;
RL Submitted (OCT-2015) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:KQW23317.1, ECO:0000313|Proteomes:UP000051348}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=Root123D2 {ECO:0000313|EMBL:KQW23317.1,
RC ECO:0000313|Proteomes:UP000051348};
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:KQW23317.1}.
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; LMDP01000001; KQW23317.1; -; Genomic_DNA.
DR RefSeq; WP_056295069.1; NZ_LMDP01000001.1.
DR AlphaFoldDB; A0A0Q6Z528; -.
DR STRING; 1736436.ASC80_08580; -.
DR OrthoDB; 8123321at2; -.
DR Proteomes; UP000051348; 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:UP000051348}.
FT DOMAIN 35..155
FT /note="Aldehyde oxidase/xanthine dehydrogenase a/b
FT hammerhead"
FT /evidence="ECO:0000259|SMART:SM01008"
SQ SEQUENCE 791 AA; 84145 MW; F8F9855A4CB0D2E3 CRC64;
MQDHPARRSQ ENDIALQKFG IGQPVRRKED DTLVRGKGRY TDDINAPGQA YAVIVRSTHA
HGRIRQIQTD EARKMPGVLG VWTGADLAAA NYTPFTTGVP LKSRDGSPVY QTNRFPLATD
KVRFVGDPVA FVVATTLAQA RDAAEAVVID VDPLPAVTNA EAASQPGAPQ LYEHIPNNVA
LDFHSGDTPA LDAAFAKAAH IARLDIANTR LAVVPMEPRA ALASFDKATQ RYVIDLPTQG
VAGNRTALAK TLNVPNDKVH LRTHNVGGSF GMKNASYPEY ICILHAAKEL GRPVKWTDER
SSSFLSDSHG RAQDVHAELA LAADGTFLGV RIQGYGNLGA YITGVAPIPL SINIAKNIAS
VYRTPLIGVD IKCVVTNTTL MGAYRGAGRP EANYFMERLI DHAADEMGID RLTLRKRNFV
KPSQIPYAAA NGLTYDSGDF QGVFAQALQL SDHANFPKRK KESRKRGKLS GIAVGSYLEI
TAPPSVELGK IQFEADGTVK LTTGTLDYGQ GHATPFAQVL AAQLGVPFEA ITLEQGDSDV
VHTGNGTGGS RSITASGTAI VEASKLVIEK GRKAAAYMLE ASEADIEFSN GRFSITGTDR
DIGIMELAAK LRDARLPDDA PHSLDVDHTS SPIASTFPNG CHVAEVEIDP DTGVVRIVRY
TGVNDFGTVV NPMIVAGQIH GGVAQGIGQA LMECVTYDDN GQPITGSFMD YAMPRATDIP
SMTLGDHPSP ATSNPLGSKG CGEAGCAGSL ATIVNAVVDA LSEFGVTHID MPLTPEKIWR
AIADGRKAKT A
//