ID A0A370U9L6_9GAMM Unreviewed; 1214 AA.
AC A0A370U9L6;
DT 07-NOV-2018, integrated into UniProtKB/TrEMBL.
DT 07-NOV-2018, sequence version 1.
DT 24-JAN-2024, entry version 14.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:RDL44479.1};
GN Name=uca {ECO:0000313|EMBL:RDL44479.1};
GN ORFNames=DN730_08760 {ECO:0000313|EMBL:RDL44479.1};
OS Marinomonas piezotolerans.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Oceanospirillales;
OC Oceanospirillaceae; Marinomonas.
OX NCBI_TaxID=2213058 {ECO:0000313|EMBL:RDL44479.1, ECO:0000313|Proteomes:UP000254326};
RN [1] {ECO:0000313|EMBL:RDL44479.1, ECO:0000313|Proteomes:UP000254326}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=YLB-05 {ECO:0000313|EMBL:RDL44479.1,
RC ECO:0000313|Proteomes:UP000254326};
RA Yu L., Tang X.;
RT "Marinomonas sp. YLB-05 draft genome sequence.";
RL Submitted (JUN-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:RDL44479.1}.
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DR EMBL; QKRA01000003; RDL44479.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A370U9L6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000254326; 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:UP000254326}.
FT DOMAIN 1..458
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 1131..1206
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1214 AA; 134065 MW; ECAB2A848CFA4CE9 CRC64;
MFHTVLIANR GAIAARIIRT LQRMNIKAVA VYAESDAKSR HVKLADEAYP LGEGAASDTY
LNVDTILRIA KASGAQAIHP GYGFLSENAN FVRRCEAEGI AFIGPTDEHM LAFGLKHRAR
ALAEQAEVPL LPGSELLTDL DSALDIAQKI GYPVMLKSTA GGGGIGMHLC HDDKELQENF
ASVKRLGASN FADDGVFLEK FIARARHIEV QVFADGQGSA LALGERDCSS QRRNQKVVEE
CPAPNLTDAV RKQLHQTAES LLASVSYRNA GTVEFIYDMD TDLFYFLEVN TRLQVEHGVT
EEVYGVDLVE WMVRLAAGEA LNLNEKRETL TPKGHSIQVR LYAEDPYKDF QPSPGLLSYV
NLPASYTESD APASEQRIRI DHWVESGIEI SPYFDPMIAK VIVHDTDRTA ALALLQSTLE
HCTLYGTQTN LDYLKQLLED KTLLNGEVST RYLNSFVYSP KRIDVLSGGT QTTLQDFPGR
QHHWNVGVPP SGPFDRYHSR LANRLLENSD DAATMEITLQ GPTLKFSFET AITLAGASID
AKLDDVALPR HEVVMVKPGQ TLTLGRIKES GARAYLAVAG GFNCPDYLGS KSTFTLGQFG
GHNGRALQTG DVLTTLDTKA PAAGTQLPSA LIPELAHHHT LRVIYGPHGC PDFFTDEDID
MFFTTDWEIH YNSSRTGVRL IGPKPKWARQ NGGEAGLHPS NIHDNAYAFG SVDFTGDMPV
ILGPDGPSLG GFVCPATVIT ADLWKLGQLR AGDTVRFVPV TLDDAVALEA EQSASIATLS
SPELTVESCG ITSPILKTLS AEQFGDDIVY RAAGDHFLLV EYGEQVLDIR LRFRAHALMQ
WLEQHPFAGM KELTPGIRSL QIHYDSQQTR HTALLELLEH AERALGEKLA ELSVPSRTVY
LPLSWDDRAC QEAIDKYAQS VRSNAPWCPS NLEFIRRING LDSIDQVKDI VFNASYLVMG
LGDVYLGAPV ATPVDPRHRL VTTKYNPART WTAENSVGIG GSYLCVYGME GPGGYQFVGR
TLQMWNRYRQ TSAFNKPWLL RFFDQIRFYE VSHDELQQIR KDFPHDNYPI RIEESSFSLS
EYEAFVDRHQ SDIDQFKTTR NQAFADELAR WHANGQFHFD QDEAEHTETD VTWSEDAVVV
DSPVSGSVWQ TQVSSGEHVK AGQLLVILES MKMEIPLHAP SDGVVSDVLL KNGSRVSAGQ
AVVVLEEPVT GESA
//
