ID A0A1N6VUX5_9GAMM Unreviewed; 1208 AA.
AC A0A1N6VUX5;
DT 15-MAR-2017, integrated into UniProtKB/TrEMBL.
DT 15-MAR-2017, sequence version 1.
DT 24-JAN-2024, entry version 21.
DE SubName: Full=Urea carboxylase {ECO:0000313|EMBL:SIQ81568.1};
GN ORFNames=SAMN05880558_1066 {ECO:0000313|EMBL:SIQ81568.1};
OS Aeromonas sp. RU39B.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Aeromonadales;
OC Aeromonadaceae; Aeromonas.
OX NCBI_TaxID=1907416 {ECO:0000313|EMBL:SIQ81568.1, ECO:0000313|Proteomes:UP000186911};
RN [1] {ECO:0000313|EMBL:SIQ81568.1, ECO:0000313|Proteomes:UP000186911}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RU39B {ECO:0000313|EMBL:SIQ81568.1,
RC ECO:0000313|Proteomes:UP000186911};
RA Mah S.A., Swanson W.J., Moy G.W., Vacquier V.D.;
RL Submitted (JAN-2017) to the EMBL/GenBank/DDBJ databases.
CC -!- COFACTOR:
CC Name=biotin; Xref=ChEBI:CHEBI:57586;
CC Evidence={ECO:0000256|ARBA:ARBA00001953};
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; FTMJ01000006; SIQ81568.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A1N6VUX5; -.
DR STRING; 1907416.SAMN05880558_1066; -.
DR InParanoid; A0A1N6VUX5; -.
DR Proteomes; UP000186911; 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}; Coiled coil {ECO:0000256|SAM:Coils};
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}.
FT DOMAIN 7..456
FT /note="Biotin carboxylation"
FT /evidence="ECO:0000259|PROSITE:PS50979"
FT DOMAIN 126..323
FT /note="ATP-grasp"
FT /evidence="ECO:0000259|PROSITE:PS50975"
FT DOMAIN 1127..1205
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
FT COILED 862..889
FT /evidence="ECO:0000256|SAM:Coils"
SQ SEQUENCE 1208 AA; 132501 MW; A3895052D30A6ACC CRC64;
MRNDPKMFSK VLIANRGAIA CRIIRTLGEM GVQSVAVYSE ADADSRHVLE ADEAWSLGEG
AAAATYLDQD KLFAIARQTG AEAIHPGYGF LSENPDFARR CEAHGLVFLG PTPEQMVAFG
LKHEARALAE AAGVPLLPGS GLLDSLEQAV VLAGQIGYPV MLKSTAGGGG IGMQRCHDEG
ELRAAYASVK RLSENNFSNG GLFLEKFIER ARHIEVQLFG DGQGEVIAIG ERDCSAQRRN
QKVIEECPAP HLADDVRLAL QQTAVRLGRQ VGYRSAGTVE YVYDESSGAF YFLEVNTRLQ
VEHGVTEQVY GIDLVRWMIE LGAGTLAPLA GLQAGLTARG HAIQVRLYAE DPAKQFRPSA
GLLSAVEFVA QDRKARRIDH WIDAGLDVPP FFDPMLAKLI GWGASRSAAL DELSAMLAGS
TVYGIETNSA YLQALLQSSL VREGRVLTRS LNEFAYQPQT IDVMSGGTQT TIQDVPGRTG
YWHIGVPPSG PMDDWSFRLG NRLLGNAPEC AGLEITLAGP TLRFNVARHI VITGAAIDAR
LDGQPLPLWQ VVMVPANATL TLGKVSGAGA RSYLLLAGGI DCPTYLGSRA TFTLGQFGGH
AGRALQAGDV LHLPPASSAS ASATLPDALI PTIGQQWTLR VIYGPHGAPD FFTEADIDTL
FASDYEVHYN SSRTGVRLIG PKPSWARRDG GEAGLHPSNL HDNAYAIGTV DFTGDMPVIL
GPDGPSLGGF VCPATLIKAD LWKMGQLKAG DRVRFVPVSL ADAERLERAK LAELESLQAQ
PLSVPVHRPA TPVLKILPAE RYGEQVVYRP SGDDYLLVEY GPQVLDIRLR FRAHALMLWL
EQAAISGVLE LTPGIRSLQI HYDNLRLPLA TLLERLEQAE SELTDIDQIT IPSRIVHLPL
SWDDEATRLA IRKYDELVRK DAPWCPSNIE FIRRINGLES IEQVREIVFS AHYLVMGLGD
VYLGAPVATP IDPRHRLVTT KYNPARTWTP ENAVGIGGAY LCVYGMEGPG GYQFVGRTLQ
MWNRYRRTAE FSQPWLLRFF DQIRFYEVDA DELLRIRREF PRGRYPLRIE ETRFSLADYN
QLVSEHGEAI TAAKERQQRA FEAERQRWQE SGQANFSADH EVLQETAQEE ELPHHHCAVE
SLVSGSVWQL QVVEGQQVRE GEPLMVIESM KMEIEVLAPV TGRVVGIVRG AGQQVRAGQR
LLVLETQG
//
