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Database: UniProt
Entry: A0A0B3BYP8_9PSED
LinkDB: A0A0B3BYP8_9PSED
Original site: A0A0B3BYP8_9PSED 
ID   A0A0B3BYP8_9PSED        Unreviewed;      1211 AA.
AC   A0A0B3BYP8;
DT   04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT   04-MAR-2015, sequence version 1.
DT   24-JAN-2024, entry version 29.
DE   SubName: Full=Urea carboxylase {ECO:0000313|EMBL:KHO64507.1};
GN   ORFNames=PT85_09870 {ECO:0000313|EMBL:KHO64507.1};
OS   Pseudomonas flexibilis.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC   Pseudomonadaceae; Pseudomonas.
OX   NCBI_TaxID=706570 {ECO:0000313|EMBL:KHO64507.1, ECO:0000313|Proteomes:UP000030980};
RN   [1] {ECO:0000313|EMBL:KHO64507.1, ECO:0000313|Proteomes:UP000030980}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=JCM 14085 {ECO:0000313|EMBL:KHO64507.1,
RC   ECO:0000313|Proteomes:UP000030980};
RA   Shin S.-K., Yi H.;
RT   "Genome sequence of Pseudomonas tuomuerensis JCM 14085.";
RL   Submitted (NOV-2014) 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:KHO64507.1}.
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DR   EMBL; JTAK01000004; KHO64507.1; -; Genomic_DNA.
DR   RefSeq; WP_039606561.1; NZ_JTAK01000004.1.
DR   AlphaFoldDB; A0A0B3BYP8; -.
DR   STRING; 706570.PT85_09870; -.
DR   OrthoDB; 9763189at2; -.
DR   Proteomes; UP000030980; 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; 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; 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};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000030980}.
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          1127..1204
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
SQ   SEQUENCE   1211 AA;  131014 MW;  55C9456C6DF7D47D CRC64;
     MFDTVLIANR GEIAVRAIRT LKRLGVKSVA VYSDADRNAQ HVRDADLAIA LGGDKPADSY
     LRVDKILAAA AETGAQAIYP GYGFLSESAE FAEACAAAGI AFVGPTPAQI REFGLKHRAR
     ELAAEAGVPM APGTGLLSSL EDALAAAERI GYPVMLKTTA GGGGIGLTRC ADAEALASAY
     ESVKRMGEQF FSDAGVFLER FVDQARHVEV QIFGDGLGRV VALGERDCSL QRRNQKVVEE
     TPAPNLPQAT RERLHAAAVQ LGSSVNYRSA GTVEFIYDAA RDDVYFLEVN TRLQVEHPVT
     ERVTGLDLIE CMLRVAAGDA LDWDALGQAP RGAAMEVRLY AEDPLKNFQP SPGALTDVHF
     PAGVRVDGWV STGSEVSAFY DPMIAKLIVH GTSREEALQK LRAALAETRL HGIASNLDYL
     RQVVADERFA EGRVWTRLLD SFQYTASVIE VLEPGTYSSV QDFPGRLGYW DIGVPPSGPM
     DDYAFRLANR IVGNHTSAAG LEFTLQGPTL KFHCDALIAL TGADCPATLD DAPVAYWEPV
     SVRAGQVLKL GRAASGCRTY LAVRNGLDVP LYLGSRSTFA LGQFGGHAGR TLRPADMLAI
     SQPALPACTT PAPVAPPQAA HASLIPSYGS TWDIGVLYGP HGAPDFFTPE AIEEFFAAEW
     EVHYNSNRLG VRLSGPKPSW TRADGGEAGL HPSNVHDCEY AIGSINFTGD FPVILTKDGP
     SLGGFVCPVT IAKAELWKVG QVKPGDRLRF HPISFQQAQA LEQAQLGSIE ALAAISAVSL
     PAPALQPGST VSATVLAELP ASAGRPQVVY RQAGDAYLLL EYGDNVLDLA LRLRVHLLME
     ALKAANIDGL AELAPGVRSL QLRYDSRVLH QRTLLDHLLR LEETLGDVSN LKVPTRIVHL
     PMAFEDSATL GAVTRYRETV RAEAPWLPNN VDFLQRINDL DSRERVKDIL YGASYLILGL
     GDVYLDAPCA VPLDPRHRLL SSKYNPARTY TAEGTVGIGG MYMCIYGMDS PGGYQLVGRT
     LPIWNKYLKN AQFERGEPWL LKFFDQVRFY EVSEEELTAF REAFREGRAQ IRIEQGEFDF
     AEYQRFLVDN AESIAAFQQR QKAAFAAEVQ LWRDDDPAAA QPLASAVEDD GDLNGHLVSA
     EMSGSVWKVL VQPGQRVEAG TPLLVVEAMK MELAVIAPVA GIVKSVRCQP GKAVTPGDAL
     LLLEPESDEA A
//
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