ID W1IPR5_9GAMM Unreviewed; 453 AA.
AC W1IPR5;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 38.
DE SubName: Full=Similar to Biotin carboxylase {ECO:0000313|EMBL:CDL79828.1};
GN ORFNames=XCR1_1250005 {ECO:0000313|EMBL:CDL79828.1};
OS Xenorhabdus cabanillasii JM26.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427517 {ECO:0000313|EMBL:CDL79828.1, ECO:0000313|Proteomes:UP000019197};
RN [1] {ECO:0000313|EMBL:CDL79828.1, ECO:0000313|Proteomes:UP000019197}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JM26 {ECO:0000313|EMBL:CDL79828.1,
RC ECO:0000313|Proteomes:UP000019197};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacterium,
RT Xenorhabdus cabanillasi strain JM26.";
RL Submitted (NOV-2013) 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:CDL79828.1}.
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; CBXE010000030; CDL79828.1; -; Genomic_DNA.
DR RefSeq; WP_038260407.1; NZ_NJGH01000060.1.
DR AlphaFoldDB; W1IPR5; -.
DR OrthoDB; 9803907at2; -.
DR Proteomes; UP000019197; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0003824; F:catalytic activity; IEA:UniProt.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF13535; ATP-grasp_4; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 128..349
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 453 AA; 51030 MW; 279B34F2C1A4D2D0 CRC64;
MKPNAILFVD VDEAEVARYT YREPHFVAAK KMGLFCLTVA HKRRQNTERL FTDSDEVFLL
ESLSFESLQD CVTRLQQSYN LCAIFCHAGH ASASGQMGCI VAEICQKIGL LYTSPASIAT
CNNKFLMRQA LQKHGIRTIR HALCNSEKEL YKQANRIGYP VMAKPPFGAS SAFIKKCYNW
FELQAHYQTF TAYYKHSASV DFLGNTQTYS TPEGTKYLNQ PGQSMLLEEY IQGIEGTVEC
AITQDTVHPV LINEKLILTE KDNTVLENLL IAPPVSFTAS EQEQIRNYAI ACIQAVGLNH
AIAHLEFRMT ADGPVVIEIN PRLGGLFVNS AFRDLAGLDP YQLYLSILLQ EKDIDTQIIQ
GQKQAATAKQ HYSMIVMYPE NSGHFLGIKN IEYIKNNPHV IECLSQPAGY DINAETEEHY
LFRCWAKVND ASHAHTLHNE MIEHVKPIVI PLS
//
