ID A0A443J502_9RHOB Unreviewed; 1167 AA.
AC A0A443J502;
DT 08-MAY-2019, integrated into UniProtKB/TrEMBL.
DT 08-MAY-2019, sequence version 1.
DT 13-SEP-2023, entry version 11.
DE SubName: Full=5-oxoprolinase/urea amidolyase family protein {ECO:0000313|EMBL:RWR15539.1};
GN ORFNames=D2T33_01310 {ECO:0000313|EMBL:RWR15539.1};
OS Sinirhodobacter populi.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Sinirhodobacter.
OX NCBI_TaxID=2306993 {ECO:0000313|EMBL:RWR15539.1, ECO:0000313|Proteomes:UP000285710};
RN [1] {ECO:0000313|EMBL:RWR15539.1, ECO:0000313|Proteomes:UP000285710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2D-5 {ECO:0000313|EMBL:RWR15539.1,
RC ECO:0000313|Proteomes:UP000285710};
RA Xu G.;
RT "Sinorhodobacter populi sp. nov. isolated from the symptomatic bark tissue
RT of Populus euramericana canker.";
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
RN [2] {ECO:0000313|EMBL:RWR15539.1, ECO:0000313|Proteomes:UP000285710}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=2D-5 {ECO:0000313|EMBL:RWR15539.1,
RC ECO:0000313|Proteomes:UP000285710};
RA Li Y.;
RL Submitted (JAN-2019) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:RWR15539.1}.
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DR EMBL; SAUW01000001; RWR15539.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A443J502; -.
DR Proteomes; UP000285710; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:RWR15539.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000285710}.
FT DOMAIN 1..443
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1087..1165
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1167 AA; 124966 MW; 36EC66AB02A43169 CRC64;
MFSKVLVANR GEIAVRILRT LKKMGIASVA VYSDADRFAP HVRLADEAVR LGPAPAAESY
LNAEAVLAAC RATGAEAVHP GYGFLSENTG FSARLAAAGI AFIGPRPEHV EAFGLKHTAR
ELAKAAGVPL LPGSGLLTDA DAAAAEAART GYPVMLKSTA GGGGIGMSLC PDEAALRAAF
AGVQRTARAS FGDARVYLER FVHDARHVEV QIFGNGAGRV IALGERDCSL QRRNQKVIEE
TPAPLLPDAV RARLHKAAAD LCARVAYASA GTVEFIYDPR RAEFYFLEVN TRLQVEHPVT
EAVFGIDLVE WMIRQAAGED PIPATMPAPQ GAAIEARLYA EMPHAGFRPS AGLLTEVVFP
DTARIDGWIE TGSEVTTFYD PMLAKIIVHA ADRPAALAGL RDALAATRVS GIETNLEYLR
AIAGSELLAS GKVATTALAA FAFAPEGIEV LSPGPQSSLQ ELPGRLGLWH VGVPPSGPMD
ARSHRNANRL LGNPPDTTTL EMTVSGPVLR FLAPARVALA GARMRLTLDG TPVEGPVVEV
PAGATLAIGA IEGPGQRAYL AVAGGFDAPE ILGSRATFAL GHFGGPAAGV LKTGDVLHIG
RAKIGPPLPP EPAGLTQDWV LSVVYGPHGA PDFFRDSDIA TLFSTAYEVH FNSARTGVRL
IGPAPDWARG DGGDAGLHPS NIHDTAYAIG AIDFTGDMPI ILGPDGPSLG GFVCPAVVTA
EDLWKLGQLR PGDRVRFRAA ERPADPVAGP ALLRMGSPVV GAVEGAVPVT YRRQGDENLL
VEYGPMVLDI ELRLRVQLLM QAVRAAGLPM IDLTPGIRSL QLHYDSMRIS RADLLAELQR
IEAALPAADQ VRVPSRTVWL PLSWNDPQAE LAMRKYQDLV RPNAPWCPSN IEFIRRINGM
EDEAEVRRTI FDARYLVMGL GDVYLGAPVA TPVDPRHRLV TTKYNPARTW TPENAVGIGG
AYMCIYGMEG PGGYQLFGRT IQVWNTWRRT AAFRDRPWLL DFFDQIRFFP VTHQELEEAR
AAFPHGGYDL RIEEGTFDWA AEKRRLADEA DSIAAFKSRQ QVAFGAERAR WKALGLDHFL
PDEGARLEGA DLPAGCIGVE SPVPGNLWKY LVAPGARVAA GDPIAILESM KMEITVPSPA
TGRLRELRAA PGRTLRAGDV LAVMETE
//
