ID A1U9I7_MYCSK Unreviewed; 221 AA.
AC A1U9I7;
DT 06-FEB-2007, integrated into UniProtKB/TrEMBL.
DT 06-FEB-2007, sequence version 1.
DT 27-MAR-2024, entry version 89.
DE SubName: Full=Allophanate hydrolase subunit 1 {ECO:0000313|EMBL:ABL89495.1};
GN OrderedLocusNames=Mkms_0278 {ECO:0000313|EMBL:ABL89495.1};
OS Mycobacterium sp. (strain KMS).
OC Bacteria; Actinomycetota; Actinomycetes; Mycobacteriales; Mycobacteriaceae;
OC Mycobacterium.
OX NCBI_TaxID=189918 {ECO:0000313|EMBL:ABL89495.1};
RN [1] {ECO:0000313|EMBL:ABL89495.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=KMS {ECO:0000313|EMBL:ABL89495.1};
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 Kiss H., Brettin T., Bruce D., Han C., Tapia R., Gilna P., Schmutz J.,
RA Larimer F., Land M., Hauser L., Kyrpides N., Mikhailova N., Miller C.D.,
RA Richardson P.;
RT "Complete sequence of chromosome of Mycobacterium sp. KMS.";
RL Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
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; CP000518; ABL89495.1; -; Genomic_DNA.
DR AlphaFoldDB; A1U9I7; -.
DR STRING; 189918.Mkms_0278; -.
DR KEGG; mkm:Mkms_0278; -.
DR HOGENOM; CLU_020207_0_1_11; -.
DR OrthoDB; 9778567at2; -.
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:ABL89495.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741}.
FT DOMAIN 14..209
FT /note="Carboxyltransferase"
FT /evidence="ECO:0000259|SMART:SM00796"
SQ SEQUENCE 221 AA; 23600 MW; 02AD7F5A18A67DA6 CRC64;
MTAVPDVMEP MVLGTVLDYG DRALLLQFDD TAQVLAWTDA VRAAGLPGVV DIVPGSRTVL
VKLDGPRYQA PTRQRLAALR IDRGAVAESA SPPDRADAVI DVVYDGADLA DVARLTGMDT
DQVVAAHTGT LWRVGFGGFA PGFAYLVGGD ERLHVPRRAE PRTKVPAGSV GLAGEFSGVY
PRESPGGWQL IGHTDAVLWD VDRENPALLT PGMWVEFRVA E
//
