ID A0A1V4CD76_9BURK Unreviewed; 1208 AA.
AC A0A1V4CD76;
DT 07-JUN-2017, integrated into UniProtKB/TrEMBL.
DT 07-JUN-2017, sequence version 1.
DT 24-JAN-2024, entry version 17.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:OPF62818.1};
GN ORFNames=BC358_11475 {ECO:0000313|EMBL:OPF62818.1};
OS Hydrogenophaga sp. H7.
OC Bacteria; Pseudomonadota; Betaproteobacteria; Burkholderiales;
OC Comamonadaceae; Hydrogenophaga.
OX NCBI_TaxID=1882399 {ECO:0000313|EMBL:OPF62818.1, ECO:0000313|Proteomes:UP000189907};
RN [1] {ECO:0000313|Proteomes:UP000189907}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=H7 {ECO:0000313|Proteomes:UP000189907};
RA Florea S., Webb J.S., Jaromczyk J., Schardl C.L.;
RL Submitted (JUL-2016) 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:OPF62818.1}.
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DR EMBL; MCIC01000016; OPF62818.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1V4CD76; -.
DR STRING; 1882399.BC358_11475; -.
DR OrthoDB; 9803706at2; -.
DR Proteomes; UP000189907; 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 GO; GO:0006164; P:purine nucleotide biosynthetic process; IEA:UniProtKB-KW.
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}; Purine biosynthesis {ECO:0000256|ARBA:ARBA00022755};
KW Reference proteome {ECO:0000313|Proteomes:UP000189907}.
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..1206
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1208 AA; 129858 MW; B7FFDAE6720B417A CRC64;
MFRKVLIANR GAIACRIIRT LKALGVQSVA VYSEADAQAR HVREADEAWL LGPAPAAESY
LKAERILQIA KDCGAEAIHP GYGFLSENPG FAQACEDAGI AFIGPTPDQM RAFGLKHTAR
DLAEQRGVPL LPGTGLLADA AQARAEALRI GYPVMLKSTA GGGGIGMRLV WSEDELSDAF
ASVQRLASAN FKDAGLFLEK YVEQARHIEV QVFGDGAGTV LALGERDCSV QRRNQKVIEE
TPAPGLSDAQ RHELHATAVR LAQAVNYRSA GTVEFVYDAA TGQFYFLEVN TRLQVEHGVT
EQVTGVDLVA WMVQLAAGDL PPLATLAPTP QGASIQVRLY AEDPAKNFQP SAGLLTEVVF
PTDARVDGWV ERGTEVPAWY DPMLAKLIVT APDREQALQK LDAALAATRL AGIETNLGYL
RQVVRDPVFR EGRQVTRFLN SFHFRPATVE VVEPGVQTSV QDWPGRLGHW DVGVPPSGPM
DAYAHRMANR LVGNAADAAA LEITLAGPTL RFNADAVIAV TGAPVKVLLD GAPLPLWQSH
RVAAGSVLAI GRAEAGARLC LAVGGGFDVP LYLGSRSTFT LGQFGGHAGR HLRTGDVLHL
AAPGAGTAGV SASSDTVPAF THHWDVGVLY GPHGAPDFFT ESDVATFFAT DWEVHYNSSR
TGVRLIGPKP HWARADGGEA GLHPSNIHDN AYAIGAIDFT GDMPVILGPD GPSLGGFVCP
AVVVDAELWK LGQLRPGDTV RFHRLSLDEA LARSASVEAA LTSLTQALPA TPADDASAHP
TPIILADPAR EDEAVPAMVV RQAGDRYLLV EFGPLVLDIE LRLRVHVLMQ ALQARIAAGT
LPGIVDMTPG IRSLQLHFDP AKVSRAELLK VLVEAEAALP AVDDMEVPSR IVHLPLSWDD
PQTKLAIEKY MQSVRPDAPW CPSNIEFIRR INGLDSIEDV FKVVFDASYL VLGLGDVYLG
APVATPVDPR HRLVTTKYNP ARTWTPENAV GIGGAYLCVY GMEGPGGYQF VGRTLQMWNR
WRHGEPGSVF EQPWLLRFFD QIRFVPVDQD ELLRIRAAFP HGGYALQIEE TSFSLRDYRR
FLADNAASIG AFKAQQQASF DAERERWAAS GQLSYAGDAD VAAADASVEL DLPPGGRPLA
SSVPGSVWKV LVSEGQRVAA GDVLLVVESM KMEFSVLAPQ DATVHRLMCR EGAPVAAGQD
VLVLVSED
//
