ID A0A0U5EWI6_9PROT Unreviewed; 1199 AA.
AC A0A0U5EWI6;
DT 16-MAR-2016, integrated into UniProtKB/TrEMBL.
DT 16-MAR-2016, sequence version 1.
DT 24-JAN-2024, entry version 23.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:CEF39976.1};
DE EC=6.3.4.6 {ECO:0000313|EMBL:CEF39976.1};
GN Name=uahA {ECO:0000313|EMBL:CEF39976.1};
GN ORFNames=ASN_561 {ECO:0000313|EMBL:CEF39976.1};
OS Acetobacter senegalensis.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC Acetobacteraceae; Acetobacter.
OX NCBI_TaxID=446692 {ECO:0000313|EMBL:CEF39976.1, ECO:0000313|Proteomes:UP000056109};
RN [1] {ECO:0000313|Proteomes:UP000056109}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=108B {ECO:0000313|Proteomes:UP000056109};
RA Illeghems K.G.;
RL Submitted (SEP-2014) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
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DR EMBL; LN606600; CEF39976.1; -; Genomic_DNA.
DR RefSeq; WP_058987082.1; NZ_LN606600.1.
DR AlphaFoldDB; A0A0U5EWI6; -.
DR GeneID; 34781750; -.
DR KEGG; asz:ASN_561; -.
DR PATRIC; fig|446692.3.peg.526; -.
DR Proteomes; UP000056109; Chromosome I.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR GO; GO:0016787; F:hydrolase activity; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR GO; GO:0004847; F:urea carboxylase activity; IEA:UniProtKB-EC.
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, ECO:0000313|EMBL:CEF39976.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}.
FT DOMAIN 1..450
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 1119..1197
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1199 AA; 130589 MW; 2D6ECDB14E06C7A1 CRC64;
MFKKLLIANR GAIAARIERT LQDLHVCSVA VYSEADLGSL HVRNADLAIS LGEGAAAETY
LKTDKILAAA RQAGAQAIHP GYGFLSENAA FAEECESQGF AFVGPTPEQL RTFGLKHTAR
DLAAAQGVPM LRGTPLLNTA QDATDAGTQI GYPVMLKSTA GGGGIGMRVC YSEEELIEAF
DKVRQLGLNN FSDGGVFIEK YIEHARHLEV QIFGDGQGEV IALGVRDCSI QRRNQKVIEE
TPAPGLPDGI AEALCEAAIR LGKATHYRSA GTVEFVYDSD VKQFYFLEVN TRLQVEHGVT
EQVWGVDLVR WMVELAAGTL PPLSTLMASL TPQGHAIQAR LYAEDPGRNF QPSPGLVTHV
HFPPADGKAL RIDTWIEAGA EIPAFFDPMV AKVIAHDSTR QAALARLDDA LAKTEIYGVE
TNCAYLRQIL AYQPFVESNP WTRCLEGLTY KANTFEVLVA GTQTTVQDFP GRLGYWAVGI
PPSGPMDSRS FQMANRLLGN AAGAAGLEIT MNGPTLRFNT DAVVAITGAE IVIELDGQPC
PMNTAFRVCA GSVLKLGSIV RKGARSYLAL RGGIVVPSYL GSCSTFILGQ FGGHAGRALR
VGDVLHLPPS QSLTDGAVLP VSLALALPDV QTVRVIYGPH AAPEYFTPAY METFFATEWE
IHFNSSRTGI RLIGPKPEWV RESGGEAGLH PSNIHDNPYA IGAVDFTGDM PVILGPDGPS
LGGFVCPVTV ISADLWKLGQ LRAGDLVRFV PVDLPTAHSL ARSGEAEVQT LEEQSPSWER
AQLSSPIVMT EGEGSTRLVA RLSGDANLLL EIGDPELDLT LRFRAHALMR AMEAENLNGI
IDLTPGIRSL QIHYASNLIT SGQLLSIIKQ LWADVLKKTN LRVPSRIVHL PLSWDDPACQ
LAIRKYMTTV RKDAPWCPSN LEFIRRINDL GSIDDVYNIV FNASYVVMGL GDVYLGAPVA
TPLDPRHRLV TTKYNPARTW TAENSVGIGG AYLCVYGMEG PGGYQFVGRT LQMWMRYRLP
EAFQGKSWLL RFFDQVRFYP VSAEELEVIR RDFPLGRYDI KIEQTEIALS DYHAFLEQHH
EAISTFQKCQ QAAFDAERQR WIENGTANFE SNDVAPEEGE DVPLANGLQA VESGIAGNLW
QVLVSLNDRV EVGQVVVVLE SMKMEISLVA PCSGTVMEIR VQPGAPVRSG QCVIVIKED
//
