ID F3C5C0_PSESG Unreviewed; 417 AA.
AC F3C5C0;
DT 28-JUN-2011, integrated into UniProtKB/TrEMBL.
DT 28-JUN-2011, sequence version 1.
DT 24-JAN-2024, entry version 45.
DE SubName: Full=Urea amidolyase-like protein {ECO:0000313|EMBL:EGH13475.1};
GN ORFNames=Pgy4_14371 {ECO:0000313|EMBL:EGH13475.1};
OS Pseudomonas savastanoi pv. glycinea str. race 4.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=875330 {ECO:0000313|EMBL:EGH13475.1, ECO:0000313|Proteomes:UP000005466};
RN [1] {ECO:0000313|EMBL:EGH13475.1, ECO:0000313|Proteomes:UP000005466}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=race 4 {ECO:0000313|Proteomes:UP000005466};
RX PubMed=21799664; DOI=10.1371/journal.ppat.1002132;
RA Baltrus D.A., Nishimura M.T., Romanchuk A., Chang J.H., Mukhtar M.S.,
RA Cherkis K., Roach J., Grant S.R., Jones C.D., Dangl J.L.;
RT "Dynamic evolution of pathogenicity revealed by sequencing and comparative
RT genomics of 19 Pseudomonas syringae isolates.";
RL PLoS Pathog. 7:E1002132-e1002132(2011).
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:EGH13475.1}.
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DR EMBL; ADWY01000643; EGH13475.1; -; Genomic_DNA.
DR AlphaFoldDB; F3C5C0; -.
DR PATRIC; fig|875330.6.peg.2486; -.
DR HOGENOM; CLU_020207_4_0_6; -.
DR BioCyc; PSYR875330:G11XH-2758-MONOMER; -.
DR Proteomes; UP000005466; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016829; F:lyase activity; IEA:UniProtKB-KW.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR010016; PxpB.
DR InterPro; IPR011053; Single_hybrid_motif.
DR PANTHER; PTHR34698; 5-OXOPROLINASE SUBUNIT B; 1.
DR PANTHER; PTHR34698:SF2; 5-OXOPROLINASE SUBUNIT B; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Lyase {ECO:0000313|EMBL:EGH13475.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 335..415
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 417 AA; 46458 MW; 76ED8C5F7AF62839 CRC64;
MPSPVILDIG QDDKRLVARL SGDTHLLLEI GAPELDLVLR LRGHALMLAL EAKQLGGVID
LTPGIRSLQV HYRPEQLPLR QLLDIVAGEW DAVCAAKDLQ VASRIVHLPL SWDDPACQLA
IEKYMTTVRK DAPWCPSNLE FIRRINDLPN LDEVQRTVFD ASYLVMGLGD VYLGAPVATP
LDPRHRLVTT KYNPARTWTA ENSVGIGGAY MCVYGMEGPG GYQFVGRTLQ MWNRYRDVAA
FEGKPWLLRF FDQIRFYPVS ADELLRIRRD FPLGRFDLNI EHSTLNMADY QAFLTREAEG
ITAFRAQQQS AFNAERERWI ANGQADFQSD EGVAPNTEEL PLQTGQQGVD SHIAGNLWQV
QVQPGERVEA GDVLVILESM KMEIPLLAPV AGVVQEVRVQ PGSAVRAGQR VVVLAAD
//
