ID A0A1I2REI0_9SPHN Unreviewed; 1201 AA.
AC A0A1I2REI0;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 16.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:SFG36271.1};
GN ORFNames=SAMN05518801_11936 {ECO:0000313|EMBL:SFG36271.1};
OS Novosphingobium sp. CF614.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Sphingomonadales;
OC Sphingomonadaceae; Novosphingobium.
OX NCBI_TaxID=1884364 {ECO:0000313|EMBL:SFG36271.1, ECO:0000313|Proteomes:UP000199304};
RN [1] {ECO:0000313|EMBL:SFG36271.1, ECO:0000313|Proteomes:UP000199304}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CF614 {ECO:0000313|EMBL:SFG36271.1,
RC ECO:0000313|Proteomes:UP000199304};
RA de Groot N.N.;
RL Submitted (OCT-2016) 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; FOOR01000019; SFG36271.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1I2REI0; -.
DR STRING; 1884364.SAMN05518801_11936; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000199304; 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; 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};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000199304}.
FT DOMAIN 2..445
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 121..318
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1120..1198
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1201 AA; 129404 MW; 1430CA5112DFC9BD CRC64;
MSFDTVLVAN RGAIATRIIR TLRQMGLRSV AVYSDADVGS LHVSQADLAV CIGPAPASES
YLDTAAILAA ARETGAGAIH PGYGFLAENA EFAESCAAGG IVFIGPTPEN IRTFGLKHSA
RALAAEHGVP LAPGTGLLTD EEEAASAARK IGYPVILKAT AGGGGIGMRI CEDEAAVREG
FAGVARLGEG NFGDAGVFLE CYVGRARHIE VQIFGDGTGR VMALGERDCS LQRRNQKVVE
EAPAPLLPAA IRAELIAAAV RLGEAARYRS AGTVEFLFDA ERQQFFFLEM NTRLQVEHGV
TEEVMGIDLV EWMIRGAAGD FSFLDAEPPM PRGHAVQVRL YAEDPALDYR PTSGTLTAVS
FPQGIRAETW CMAGTAISAW YDPMLAKLIV HAPTREAAIS AMQAALDESR IDGIETNLRW
LREVVRTGPF VDGEVSTRLL DTVAYRPRSI RVIGGGTATT VQDWPGRQGL WAIGVPPSGP
MDDKSFRIGN RLLGNAEGTA GLEITVSGPT LFFNAPARLC LTGADFGARL DGTPIERGIA
VDVMAGQTLA LGSVGGGGMR GYILFAGGLD IAPYLQSHST FELGQFGGHA ARRLLAGDTL
HLGGTDVGTP PAPLPVPPFA DTWTLRVLYG PHGAPDFFTD DDINVILAAD WQVHYNSNRT
GVRLVGPKPQ WARTDGGEAG LHPSNIHDNP YAIGAVDFTG DMPIILGPDG PSLGGFVCPF
VVIAADRWKI GQLAPGDRLR FVPVTLEDAA AADQVPLMSV PAEISSPEEP SRDIDTLSPI
LADIPGQGTR PRVVYRQQGD RNILVEYGPI VLDIELRIRV HALMAELEQL ALPGVIDIVP
GIRSLQLHFD GRVLDQRGAL AALMEAEERL GDLEDFSVPS RIVHLPLSWR DPATIETIEK
YMGAVRDDAP WCPDNIEFIR RINGLSDADA VESIVFDASY LVLGLGDVYL GAPVATPVDP
RHRLVTTKYN PARTWTPPNV VGIGGAYMCI YGMEGPGGYQ LFGRTIQIWN THRQTDAFIE
GKPWLLRFFD QIRFFKVSAE ELAEWRRDFP SGRRSIPVEQ SEFRLADYRA FLAENRASIT
SFEARRQAAF DEERAEWQRG GEFDRVTDLA DDAETGALPM AAIEVPDGAD LIEAPFGGSV
WKLLVAPGDK VKTGDIIAVI EAMKMECPLE SPGSGTIAAL YMQERQSLQP GAPMLALRRH
P
//
