ID W1IZD6_9GAMM Unreviewed; 399 AA.
AC W1IZD6;
DT 19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT 19-MAR-2014, sequence version 1.
DT 27-MAR-2024, entry version 25.
DE SubName: Full=Biotin carboxylase {ECO:0000313|EMBL:CDL83819.1};
GN ORFNames=XSR1_370034 {ECO:0000313|EMBL:CDL83819.1};
OS Xenorhabdus szentirmaii DSM 16338.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=1427518 {ECO:0000313|EMBL:CDL83819.1, ECO:0000313|Proteomes:UP000019202};
RN [1] {ECO:0000313|EMBL:CDL83819.1, ECO:0000313|Proteomes:UP000019202}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 16338 {ECO:0000313|EMBL:CDL83819.1,
RC ECO:0000313|Proteomes:UP000019202};
RA Gualtieri M., Ogier J.C., Pages S., Givaudan A., Gaudriault S.;
RT "Draft genome sequence and annotation of the entomopathogenic bacteria,
RT Xenorhabdus cabanillasi strain JM26 and Xenorhabdus szentirmai strain DSM
RT 16338.";
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:CDL83819.1}.
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DR EMBL; CBXF010000096; CDL83819.1; -; Genomic_DNA.
DR RefSeq; WP_038239458.1; NZ_NIBV01000002.1.
DR AlphaFoldDB; W1IZD6; -.
DR STRING; 1427518.XSR1_370034; -.
DR OrthoDB; 6951671at2; -.
DR Proteomes; UP000019202; 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; 3.40.50.20; -; 1.
DR Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR003806; ATP-grasp_PylC-type.
DR InterPro; IPR013815; ATP_grasp_subdomain_1.
DR PANTHER; PTHR43585:SF2; ATP-GRASP ENZYME FSQD; 1.
DR PANTHER; PTHR43585; FUMIPYRROLE BIOSYNTHESIS PROTEIN C; 1.
DR Pfam; PF02655; ATP-grasp_3; 1.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR PROSITE; PS50975; ATP_GRASP; 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}; Reference proteome {ECO:0000313|Proteomes:UP000019202}.
FT DOMAIN 113..310
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
SQ SEQUENCE 399 AA; 45159 MW; C2A1B6DFC08D503A CRC64;
MTHILIINRY DDELSDYKKY INHREAHVSY ISLQGKTRLI DPAVSAEVCE VEQLDPNVVY
QEATRIHCNR PIDFVIAFSE YDLDTAAKIR TELNIRGAKI SDNLLCRNKT SMKEALLGSS
VRYPQYRQVA SRQEIEAFCL EKARPVILKP QVGAASDGVV KIEKLADIPD LLDFSGYEVE
EFIEGEIYHV DAILSGNTIP DPNTRPYSST MPYFKVSKYI NTCLDFRNAM PLGSVTVDDP
EFISKVRLFT EEVCHRMHLK DQAIHLEFIK SNEELVFLEV GGRVGGGEIP FITLSHESVD
LFEMWFQAAL GISLAPVNTK ITGFLMMPNP FKTGFAFEPN MTLCHPLITY QNIKQSGEYS
SFSYDDIPAR VHFMGESQAA VEEAIIHCME TLQRAIHAV
//
