ID A0A069D9N0_9BACL Unreviewed; 1205 AA.
AC A0A069D9N0;
DT 01-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 01-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 28.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:GAK39060.1};
GN ORFNames=TCA2_1548 {ECO:0000313|EMBL:GAK39060.1};
OS Paenibacillus sp. TCA20.
OC Bacteria; Bacillota; Bacilli; Bacillales; Paenibacillaceae; Paenibacillus.
OX NCBI_TaxID=1499968 {ECO:0000313|EMBL:GAK39060.1, ECO:0000313|Proteomes:UP000028160};
RN [1] {ECO:0000313|EMBL:GAK39060.1, ECO:0000313|Proteomes:UP000028160}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=TCA20 {ECO:0000313|EMBL:GAK39060.1,
RC ECO:0000313|Proteomes:UP000028160};
RA Fujinami S., Takeda-Yano K., Onodera T., Satoh K., Sano M., Takahashi Y.,
RA Narumi I., Ito M.;
RT "Draft Genome Sequence of Calcium-Dependent Paenibacillus sp. Strain TCA20,
RT Isolated from a Hot Spring Containing a High Concentration of Calcium
RT Ions.";
RL Genome Announc. 2:e00866-14(2014).
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:GAK39060.1}.
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DR EMBL; BBIW01000002; GAK39060.1; -; Genomic_DNA.
DR RefSeq; WP_047910282.1; NZ_BBIW01000002.1.
DR AlphaFoldDB; A0A069D9N0; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR eggNOG; COG4770; Bacteria.
DR OrthoDB; 9807469at2; -.
DR Proteomes; UP000028160; 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:UP000028160}.
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 1118..1196
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1205 AA; 132988 MW; 571622020E704FB4 CRC64;
MFKKVLVANR GAIAVRIIRT LKKMGISSVA VYTKADRDSL HVEHADEAVL IGDGPAKESY
VNAELILKTA LESGADAIHP GYGFLSENAS FAQACADHGI VFIGPSAEHI ELFGLKHTAR
AMAEKAGVPL LPGTGLIDTV EAAIQQAAAI GYPVMLKSTA GGGGIGMRIC EDETVLRAAF
DSVTRLAISN FNDGGVFLEK YIARARHVEV QIFGSSNGEA AALGERDCSV QRRNQKIIEE
TPAPQLPDHV RSAMLNSSRR LAMTAGYRNA GTVEFLYDPE HEQYYFLEVN TRLQVEHGVT
EEVLGIDLVE WMVKEAANEL DILNTDMPQS KGHSLQVRLY AEDCVHDFRP SDGRIDAIHW
PEGVRVESWI QKGVEITTLY DPMLAKLIVH ADTRSEAIAR MIEALQRLRI YGITTNQSYI
EAFLQTELFQ KGEVYTRMLG GFMPEERAIE VLGGGVQTTV QDVPGRTGYW DIGVPPSGPM
DRLAFRIGNK LLGNKEEAPG LELTLRGGEY LFREKITFCI TGADMGAELN GVPIELYTPT
VAPAGAILKF GEAKQGMRAY LLVAGGLDMP LTLGSASTFT LGGFGGHTGS ALRAGAVIRV
SSQTDGGTLQ PLAEGSRPIY TREWTIGVIP GPHCTSEYLL PAYLDQLTET EWEVHFNSSR
TGVRLIGPAP LWAREDGGDA GLHPSNIHDN AYAVGALDLT GDMPILLGPD GPSLGGFVCP
VTTASAELWK IGQLSPGDKV RFQLITIEEA EQLRYEQEQY LNSLSRDSVL PLLPEHSTGE
YMPVLAFDEE HRRFPITVRC SGDENILIEY GERELNLLYR FQVYVLMQTL QDSGDIPYIE
MTPGIRSLQV HLDASRMTVK EAAARIMEID LQLPELESIE VPSRIVKLPL SWDDPATRLA
IERYQQNVRP DAPWCPSNLE FIRRMNGLGS LEEVAEIVFN ASYLVMGLGD VYLGAPVAVP
LDPRHRLVTT KYNPARTWTP ENAVGIGGAY LCVYGMEGPG GYQFVGRTVQ MWNKFRETDN
FEQGKPWLLR FFDQLRFYPV SEDELLQMRE DFPRGEFKVE VEETTFKLGE YLHWLESIEN
ESSEFRHQQQ SAFQAERAYW KELGIAEYLA EPEVHASFGE EDLPEGSLGV NSSMSGSVWK
VLVEEGQQVK KGDTIIIEES MKMEFPQTAP FDGIISSIYV TSGDQVRSGD CIAAITPVEQ
EATAS
//
