ID A0A1H8VUV6_9GAMM Unreviewed; 1197 AA.
AC A0A1H8VUV6;
DT 22-NOV-2017, integrated into UniProtKB/TrEMBL.
DT 22-NOV-2017, sequence version 1.
DT 24-JAN-2024, entry version 18.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:SEP19073.1};
GN ORFNames=SAMN04488052_1165 {ECO:0000313|EMBL:SEP19073.1};
OS Aquisalimonas asiatica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Chromatiales;
OC Ectothiorhodospiraceae; Aquisalimonas.
OX NCBI_TaxID=406100 {ECO:0000313|EMBL:SEP19073.1, ECO:0000313|Proteomes:UP000199657};
RN [1] {ECO:0000313|EMBL:SEP19073.1, ECO:0000313|Proteomes:UP000199657}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=CGMCC 1.6291 {ECO:0000313|EMBL:SEP19073.1,
RC ECO:0000313|Proteomes:UP000199657};
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; FOEG01000016; SEP19073.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1H8VUV6; -.
DR STRING; 406100.SAMN04488052_1165; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000199657; 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:UP000199657}.
FT DOMAIN 1..445
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 1117..1193
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1197 AA; 130951 MW; B0C6C71BBD46B089 CRC64;
MFNKVLIANR GAIACRIMRT LKRLGIQSVA VYSEADRHSL HVRQADQAVH IGESAASASY
LNGDRILQVA KETGAEAIHP GYGFLSENAD FADACEAAGI AFIGPTGQQM RDFGLKHTAR
RLAEENSVPM LPGTGLLESL DEAVSAAERI GYPVMLKSTA GGGGIGMQLC HGEQDLRDAY
DSVKRLSQNN FSNSGLFLEK FVQRARHIEV QLFGDGRGGV IALGERDCSL QRRNQKVVEE
TPAPNISDAV RADLLAAAET LGRGVNYRSA GTVEYIFDAD TGEFYFLEVN TRLQVEHGVT
EAVTGVDLVE WMVRGAAGDL PDLETLRPGR PDGHAIQVRL YAEDPGKSFQ PSTGLLTEVV
FPEDARVDTW VERGSEISPW YDPMIAKVIV HAADRAAAIE AMHQALGVTE LHGLETNLRY
LRQVVADDTF GRGEVTTQYL NGFSYHAATI DVVSPGTQTT VQDWPGRVGY WDIGVPPSGP
MDSLAFRMGN RIVGNDEGAA GLELTVTGPS LRFNTDAVIA LTGAAMRAQL DGEPVPFWRP
VMVTAGQTLK MGPVQGAGVR AYLLVAGGLD VPLHMGSRAT FTLGQMGGHG ARALQPGDVL
HIGGTESVNA AIPRDEALPE YGHHWTIRTV YGPHGAPDFF TPNDIDTFFG TDWEIHYNSS
RTGVRLVGPK PEWAREDGGE AGLHPSNIHD NAYAIGTIDF TGDMPVILGP DGPSLGGFVC
PATIVSADLW KMGQLKPGDT VRFVAVSVDE ANRLEAAQDD AIQALQAPEH DAEPAPVTTP
ILRDERGNGH PLGVTYRPAG DKYLLVEYGP IELDLNLRFR VQALLEWLVE QGITGITEMT
PGVRSLQIHY EPKQLPLARL MQLLEQAEAE LKDLSEAELP SRIIHLPLAW DDSQTQLATQ
KYMQSVRSDA PWCPRNIEFI RRINGLDSEA DVKRIVFDAS YLVMGLGDVY LSAPLATPVD
PRHRLVTTKY NPARTWTPEN AVGIGGSYMC IYGMEGPGGY QFVGRTLQIW NRYKVTPEFQ
QPWLLRFFDQ IRFYEVTEDE LLAMRDAFPK GGLRIDIEET TFSLKRYNAF LAANRDSIET
FKTRQQAAFE AERQRWIESG QANYEADAEP PTPEPDAVEL ADGEYAVEGH VHGSLWALDV
QAGDRVEEDQ QLLVLESMKM EIPVMAEAAG TVRQVSCSEG DQVTPGQVLL VIAEDPR
//
