ID W7QAL2_9ALTE Unreviewed; 1204 AA.
AC W7QAL2;
DT 16-APR-2014, integrated into UniProtKB/TrEMBL.
DT 16-APR-2014, sequence version 1.
DT 24-JAN-2024, entry version 31.
DE SubName: Full=Urea amidolyase-like protein {ECO:0000313|EMBL:EWH09056.1};
GN ORFNames=DS2_14329 {ECO:0000313|EMBL:EWH09056.1};
OS Catenovulum agarivorans DS-2.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Alteromonadaceae; Catenovulum.
OX NCBI_TaxID=1328313 {ECO:0000313|EMBL:EWH09056.1, ECO:0000313|Proteomes:UP000019276};
RN [1] {ECO:0000313|EMBL:EWH09056.1, ECO:0000313|Proteomes:UP000019276}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DS-2 {ECO:0000313|EMBL:EWH09056.1,
RC ECO:0000313|Proteomes:UP000019276};
RX PubMed=24604650;
RA Shan D., Li X., Gu Z., Wei G., Gao Z., Shao Z.;
RT "Draft Genome Sequence of the Agar-Degrading Bacterium Catenovulum sp.
RT Strain DS-2, Isolated from Intestines of Haliotis diversicolor.";
RL Genome Announc. 2:e00144-14(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:EWH09056.1}.
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DR EMBL; ARZY01000030; EWH09056.1; -; Genomic_DNA.
DR RefSeq; WP_035015521.1; NZ_ARZY01000030.1.
DR AlphaFoldDB; W7QAL2; -.
DR STRING; 1328313.DS2_14329; -.
DR PATRIC; fig|1328313.3.peg.2921; -.
DR eggNOG; COG0439; Bacteria.
DR eggNOG; COG1984; Bacteria.
DR eggNOG; COG2049; Bacteria.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000019276; 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:0016829; F:lyase 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 Lyase {ECO:0000313|EMBL:EWH09056.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000019276}.
FT DOMAIN 1..451
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 1124..1202
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1204 AA; 132769 MW; 80ABB94EDBD22D2F CRC64;
MFNTVLIANR GAIASRIIRT LKQLGIKSIA VYAEADKESL HVTQADEAYS LGDGAAATTY
LNQQKIIDIA KQSGAQAIHP GYGFLSENAT FAEKLQQLNI SFIGPRAQQM IDFGLKHQAR
EIAQQANVPL VPGSGLIADL AELVAYAKEV GFPVMLKSTA GGGGIGMQKC DSIAELEKAF
INVKHLGAQN FANDGVFVEK FVEKARHIEV QVIGNGFGQV VTLGERDCSS QRRNQKVIEE
TPAPNLPEAT RSAMLTTAKN LMASVDYLNA GTVEFIYDHD QDKFYFLEVN TRLQVEHGVT
EMCYQVDLVE WMLKVAFSES VLNEATDLSC LETLKPIGHA IQARIYAENP AKNFQPSAGL
LTQVEWPTEN ARVDHWVEAG LTVSPFFDPM LAKVIVHANN RHAAIAKLDN ALTNTKLYGV
VSNIDYVQQV LANESFLQGK IFTRSLNDFK ANFTGFEVLK AGTMTTIQDY PARTGYWDIG
VPPSGPFDFY SFQLANRLLN NSTNAAGLEI TLQGPTLKFY HDCQVAISGA EVEITLDDQA
QNNHQVIAIK AGQTLKIGKV TAAGARAYLA VSGGIQCPDY LGSKSTFTLG QFGGHCGRAL
RIGDFLSIKK SANQLNNTTV SQIPADVVAP LTNNWTVRVV YGPHGAPDFF IEQDIQTIQS
HTWKIHYNSS RTGIRLIGPK PQWARETGGE AGLHPSNIHD NAYAFGTVDF TGDMPVILGP
DGPSLGGFVC PFTVIAADLW KLGQLKAGDN LNFEVVDLPT AKQIEIAQNN QIENLTNQTI
SYAPATINTP ILDTLETDDG EPNLVFRAAG DKFLLAEYGE LVLDLTLRAR VQALLEALQA
KNIMGVLELT PGIRSLQIHY DNLTVDVYQL IQMIKDIDLS LGDTRQLSFE SRIVHLPLSW
NDIACQQAID KYVQSVRKDA PWCPSNLEFI KRINGLESIE QVKDIVFNAH YLVLGLGDVY
LGAPVATPLD KCHRLVTTKY NPARTWTAEN SVGIGGAYMC IYGMEGPGGY QFVGRTVQMW
NRYRSNEVFS QPWLLRFFDQ VKYYPVSHEE LTQIRQDFPL GKWQPKIESA TVSMPELIKQ
WKTNEAEIAQ FTQQREQAFS AEMAEWKRTG ALNYSFEADA QTKTEQIQLT DKQYLMEATA
AGSVWKVSCQ TNQQVSSGES MIVLESMKME IDIAATESAK VIKVLVKEGQ QVQAGQALMI
LEEA
//
