ID A0A3D9UHA3_9GAMM Unreviewed; 1218 AA.
AC A0A3D9UHA3;
DT 16-JAN-2019, integrated into UniProtKB/TrEMBL.
DT 16-JAN-2019, sequence version 1.
DT 24-JAN-2024, entry version 20.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:REF26025.1};
GN ORFNames=BDD26_0584 {ECO:0000313|EMBL:REF26025.1};
OS Xenorhabdus cabanillasii.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Morganellaceae; Xenorhabdus.
OX NCBI_TaxID=351673 {ECO:0000313|EMBL:REF26025.1, ECO:0000313|Proteomes:UP000256294};
RN [1] {ECO:0000313|EMBL:REF26025.1, ECO:0000313|Proteomes:UP000256294}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 17905 {ECO:0000313|EMBL:REF26025.1,
RC ECO:0000313|Proteomes:UP000256294};
RA Goeker M.;
RT "Genomic Encyclopedia of Archaeal and Bacterial Type Strains, Phase II
RT (KMG-II): from individual species to whole genera.";
RL Submitted (AUG-2018) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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:REF26025.1}.
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DR EMBL; QTUB01000001; REF26025.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3D9UHA3; -.
DR Proteomes; UP000256294; Unassembled WGS sequence.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR CDD; cd06850; biotinyl_domain; 1.
DR Gene3D; 2.40.50.100; -; 1.
DR Gene3D; 3.30.1360.40; -; 1.
DR Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 1.
DR Gene3D; 2.40.100.10; Cyclophilin-like; 2.
DR InterPro; IPR011761; ATP-grasp.
DR InterPro; IPR005481; BC-like_N.
DR InterPro; IPR011764; Biotin_carboxylation_dom.
DR InterPro; IPR005482; Biotin_COase_C.
DR InterPro; IPR000089; Biotin_lipoyl.
DR InterPro; IPR005479; CbamoylP_synth_lsu-like_ATP-bd.
DR InterPro; IPR003778; CT_A_B.
DR InterPro; IPR003833; CT_C_D.
DR InterPro; IPR029000; Cyclophilin-like_dom_sf.
DR InterPro; IPR016185; PreATP-grasp_dom_sf.
DR InterPro; IPR011054; Rudment_hybrid_motif.
DR InterPro; IPR011053; Single_hybrid_motif.
DR InterPro; IPR014084; Urea_COase.
DR NCBIfam; TIGR00724; urea_amlyse_rel; 1.
DR NCBIfam; TIGR02712; urea_carbox; 1.
DR PANTHER; PTHR18866; CARBOXYLASE:PYRUVATE/ACETYL-COA/PROPIONYL-COA CARBOXYLASE; 1.
DR PANTHER; PTHR18866:SF33; METHYLCROTONOYL-COA CARBOXYLASE SUBUNIT ALPHA, MITOCHONDRIAL-RELATED; 1.
DR Pfam; PF02785; Biotin_carb_C; 1.
DR Pfam; PF00289; Biotin_carb_N; 1.
DR Pfam; PF00364; Biotin_lipoyl; 1.
DR Pfam; PF02786; CPSase_L_D2; 1.
DR Pfam; PF02626; CT_A_B; 1.
DR Pfam; PF02682; CT_C_D; 1.
DR SMART; SM00796; AHS1; 1.
DR SMART; SM00797; AHS2; 1.
DR SMART; SM00878; Biotin_carb_C; 1.
DR SUPFAM; SSF50891; Cyclophilin-like; 2.
DR SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 1.
DR SUPFAM; SSF160467; PH0987 N-terminal domain-like; 1.
DR SUPFAM; SSF52440; PreATP-grasp domain; 1.
DR SUPFAM; SSF51246; Rudiment single hybrid motif; 1.
DR SUPFAM; SSF51230; Single hybrid motif; 1.
DR PROSITE; PS50975; ATP_GRASP; 1.
DR PROSITE; PS50979; BC; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00866; CPSASE_1; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000256294}.
FT DOMAIN 1..449
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 120..317
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1138..1214
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1218 AA; 134689 MW; 244EEDE01CA32554 CRC64;
MFKTVLIANR GEIACRAIRT LKRLGIVSVA VYSDADKNSQ HVKAADIALP LNGGKACESY
LCIDKIINAA RQSRAEAIWP GYGFLSESVL FAEACEKAGI VFVGPTSQQI GEFGLKHRAR
ELAAEAGVPM TPGTGLLNSL NEALSAAEVI GYPVMLKSTA GGGGIGLSHC DDANELRQAW
ESVRHLGEQF FSDAGVFLER CIRQARHIEV QIFGDGKGNV VALGERDCSL QRRNQKVVEE
APAPNLSEQI RTKLLASAVQ LGKSVNYRSA GTVEYIYDVE QDEFYFLEVN TRLQVEHPVT
ECVTGLDLVE CMLRVAADLP VNWQYLKRAP VGTAIEVRLY AENPLKNFQP SPGVLTEVKF
PDDVHIEGVR IDSGVSTGSE VSAFYDPMIA KMIVYGENRD KALNKLREAL DCCQLHGITT
NLEYLRQITA SEPFQKGQVW TRMLDNFEPH ANIIEVLQPG TWSSIQDYPG RLGYWDIGVP
PSGPMDDFAF RLANRIVGNH ESAAGLEITL AGPTLQFHCD TLIALTGADC PALLDGKAVL
YWQPLHVKTG QVLAFGRTQS GCRTYLAVRN GFDVPCYLAS RSTFALGQFG GHAGRTLKIA
DMLPISQPSL PACTTPAPVS TPQALDPALI PVYGEKWHIG VLHGPHSAPD FFAQNYMDEF
FSSEWQVHYN SNRLGVRLMG PKPVWGRHDG GEAGLHPSNI HDCEYAIGSI NFTGDFPVIL
TRDGPSLGGF VCPVTIAKAE LWKVGQVRPG DRIRFYSITI EEAAALEEQQ NRAITTLKSV
PLPNQTAVSD TPLSVSEEER CGAVLAAIAA TDSAPAVVYR QAGDSYILIE YGENVLDLAL
RLRVHLLMDK LHDLAEAGIK EIAPGVRSLQ VRYDNQQIDQ QRLVALLLSL EEQLGDVSAM
KVPSRIIHLP MAFEDSATLG AVSRYQDTVR TRAPWLPNNV DFIQRINGLP DRETVRHIIF
DASYLILGLG DVYLGAPCAV PIDPRHRLLS SKYNPARTFT AEGTVGIGGM YMCIYGMDSP
GGYQLVGRTL PIWNKFLKNE QFAKDKPWLL RFFDQIRFYP VSEQELGQLR EDFREGRTAI
RIEETQFDFA EHLRFLQENA EDIARFKQRQ TVAFETEIKH WQQEGESSVL NIEKQPKEVD
INESGVQVSA DMNGNIWKIL VKPGDEVTKR QPLIIVEAMK MELVIYAPQS GRIKRISCQP
GHQVSPGDAL LWLELESI
//
