ID A1T1V3_MYCVP Unreviewed; 235 AA.
AC A1T1V3;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 24-JAN-2024, entry version 84.
DE SubName: Full=Allophanate hydrolase subunit 1 {ECO:0000313|EMBL:ABM11153.1};
GN OrderedLocusNames=Mvan_0304 {ECO:0000313|EMBL:ABM11153.1};
OS Mycolicibacterium vanbaalenii (strain DSM 7251 / JCM 13017 / BCRC 16820 /
OS KCTC 9966 / NRRL B-24157 / PYR-1) (Mycobacterium vanbaalenii).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycolicibacterium.
OX NCBI_TaxID=350058 {ECO:0000313|EMBL:ABM11153.1, ECO:0000313|Proteomes:UP000009159};
RN [1] {ECO:0000313|EMBL:ABM11153.1, ECO:0000313|Proteomes:UP000009159}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 7251 / JCM 13017 / BCRC 16820 / KCTC 9966 / NRRL B-24157 /
RC PYR-1 {ECO:0000313|Proteomes:UP000009159};
RG US DOE Joint Genome Institute;
RA Copeland A., Lucas S., Lapidus A., Barry K., Detter J.C.,
RA Glavina del Rio T., Hammon N., Israni S., Dalin E., Tice H., Pitluck S.,
RA Singan V., Schmutz J., Larimer F., Land M., Hauser L., Kyrpides N.,
RA Anderson I.J., Miller C., Richardson P.;
RT "Complete sequence of Mycobacterium vanbaalenii PYR-1.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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DR EMBL; CP000511; ABM11153.1; -; Genomic_DNA.
DR RefSeq; WP_011777626.1; NZ_JACKSD010000165.1.
DR AlphaFoldDB; A1T1V3; -.
DR STRING; 350058.Mvan_0304; -.
DR KEGG; mva:Mvan_0304; -.
DR eggNOG; COG2049; Bacteria.
DR HOGENOM; CLU_020207_0_1_11; -.
DR OMA; QPGFAYM; -.
DR Proteomes; UP000009159; Chromosome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 1.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR010016; PxpB.
DR PANTHER; PTHR34698; 5-OXOPROLINASE SUBUNIT B; 1.
DR PANTHER; PTHR34698:SF2; 5-OXOPROLINASE SUBUNIT B; 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.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801, ECO:0000313|EMBL:ABM11153.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 17..211
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000259|SMART:SM00796"
SQ SEQUENCE 235 AA; 25107 MW; 4775F8C460E10441 CRC64;
MSVTADAIHT VRTGGVQKIL DYGDRALLLE FDGSAEVLAW TDAVRAADLP GVEDVVPAAR
TVLVKLAGSR YRAPTRQRLA AVRPTAQALA ESTAPDTPDA VIDVVYDGED LDEVARLTGL
SRDEVIAAHT GRLWRVGFCG FAPGFAYLVG GDERLAVPRR PEPRTKVPVG SVGLAGEFTG
VYPRESPGGW QLIGRTSAVM WDVHRKDPAL LTPGMWVRFQ AADADARSSS AEVTS
//