ID A0A3R8ZTY5_9GAMM Unreviewed; 1204 AA.
AC A0A3R8ZTY5;
DT 10-APR-2019, integrated into UniProtKB/TrEMBL.
DT 10-APR-2019, sequence version 1.
DT 13-SEP-2023, entry version 14.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:RRZ88146.1};
DE EC=6.3.4.6 {ECO:0000313|EMBL:RRZ88146.1};
GN Name=uca {ECO:0000313|EMBL:RRZ88146.1};
GN ORFNames=EGK14_18350 {ECO:0000313|EMBL:RRZ88146.1};
OS Erwinia sp. 198.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Enterobacterales;
OC Erwiniaceae; Erwinia.
OX NCBI_TaxID=2022746 {ECO:0000313|EMBL:RRZ88146.1, ECO:0000313|Proteomes:UP000273595};
RN [1] {ECO:0000313|EMBL:RRZ88146.1, ECO:0000313|Proteomes:UP000273595}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=198 {ECO:0000313|EMBL:RRZ88146.1,
RC ECO:0000313|Proteomes:UP000273595};
RA D'Souza A.W., Potter R.F., Wallace M., Shupe A., Patel S., Sun S., Gul D.,
RA Kwon J.H., Andleeb S., Burnham C.-A.D., Dantas G.;
RT "Transmission dynamics of multidrug resistant bacteria on intensive care
RT unit surfaces.";
RL Submitted (OCT-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:RRZ88146.1}.
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DR EMBL; RHUM01000014; RRZ88146.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A3R8ZTY5; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000273595; 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: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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 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}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:RRZ88146.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000273595}.
FT DOMAIN 1..444
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..1204
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1204 AA; 131493 MW; E94579BAA62ED6D2 CRC64;
MFNTVLVANR GEIACRALRT LKKLGITGVA VYSDADKNAQ HVKEADIAIA LGGEKAADSY
LRIDRILAAA QQSGAQAIWP GYGFLSESLP FAAACEAANI VFVGPTAQQI GEFGLKHRAR
ELAAEAGVPM TPGTPLLNSL AEALTAADII GYPVMLKSTA GGGGIGLTRC GDAQALRGAW
ESVRRLGEQF FSDAGVFLER CIDRARHVEV QIFGDGKGKV VALGERDCSL QRRNQKVVEE
TPAPNLPEAT RRALLESAVR LGERVNYRSA GTVEYIYDAQ RDEFFFLEVN TRLQVEHPVT
ECVTGLDLVE CMLQVAAGVE PDWARMAQAP QGAAIEVRLY AEDPVKHFQP SPGVLTDVCF
PEGIRVDSGV TTGSEVPAFY DPMIAKLIVH AENRDAALAK MREALNETRL HGIATNLDYL
RQVIATDEFC SGQVWTRQLD SFTPVAHVIE VLQPGTWSSI QDYPGRPGYW DIGVPPSGPM
DDFAFRLANR IVGNAEEAAG LEFTLQGPTL RFHTDAVIAL TGADCPATLD AAPVVYWQPV
AVKAGQTLTL GRARTGCRTY LAVRNGFDVP EYLGSRSTFA LGQFGGHAGR TLRVADMLPV
SQPQLAACTT PAPVGEPQAV DAALIPTYGD EWRIGVLYGP HGAPDFFTRR SIDEFFAQSW
QVHYNSNRLG VRLAGPKPDW ARPNGGEAGL HPSNVHDCEY AIGAVNFTGD FPVILTRDGP
SLGGFVCPVT IAKAELWKVG QVKPGDRIRF HPISFDEAQA LEKAQEARIS TLHNVTAPAF
AMPSLAETAY GSATILAALA ATASTPAAVY RQAGDNYILL EYGDNVLDLA LRLRVHLLMI
ALRETGQPGM EELSPGVRSL QIRYDSRILS QKQLLALLLR VEKELGDVSR LRVPSRIVHL
PMAFEDSATL GAVERYKETV RASAPWLPNN VDFIQRINGL PTREAVRQTL FDASYLILGL
GDVYLGAPCA IPVDPRHRLL SSKYNPARTF TAEGTVGIGG MYMCIYGMDS PGGYQLVGRT
LPIWNRFLKN DQFAANEPWL LRFFDQVRFY PVSETELDRL REDFREGRGR IAMEDTFFDF
AEHTRFLQEH AADIAGFRQR QASAFETEVA LWAQEEEGAP LTSEETLLPQ EEEDGLPISA
DLSGNIWKVL VRPGDEVAVG QPLIVVEAMK MELSVNAPQA GRVRRIVCQP GRPVRPGDAL
LWLE
//
