ID A0A077LNH1_9PSED Unreviewed; 1209 AA.
AC A0A077LNH1;
DT 29-OCT-2014, integrated into UniProtKB/TrEMBL.
DT 29-OCT-2014, sequence version 1.
DT 24-JAN-2024, entry version 34.
DE SubName: Full=Urea amidolyase-like protein {ECO:0000313|EMBL:BAP45472.1};
GN ORFNames=PSCI_4770 {ECO:0000313|EMBL:BAP45472.1};
OS Pseudomonas sp. StFLB209.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=1028989 {ECO:0000313|EMBL:BAP45472.1, ECO:0000313|Proteomes:UP000031652};
RN [1] {ECO:0000313|EMBL:BAP45472.1, ECO:0000313|Proteomes:UP000031652}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=StFLB209 {ECO:0000313|EMBL:BAP45472.1,
RC ECO:0000313|Proteomes:UP000031652};
RX PubMed=25323715; DOI=10.1128/genomeA.01037-14;
RA Morohoshi T., Kato T., Someya N., Ikeda T.;
RT "Complete Genome Sequence of N-Acylhomoserine Lactone-Producing Pseudomonas
RT sp. Strain StFLB209, Isolated from Potato Phyllosphere.";
RL Genome Announc. 2:e01037-e01014(2014).
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; AP014637; BAP45472.1; -; Genomic_DNA.
DR RefSeq; WP_045491831.1; NZ_AP014637.1.
DR AlphaFoldDB; A0A077LNH1; -.
DR STRING; 1028989.PSCI_4770; -.
DR KEGG; pses:PSCI_4770; -.
DR HOGENOM; CLU_002162_0_1_6; -.
DR OrthoDB; 9763189at2; -.
DR Proteomes; UP000031652; Chromosome.
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; IPR001882; Biotin_BS.
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; PS00188; BIOTIN; 1.
DR PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
DR PROSITE; PS00867; CPSASE_2; 1.
PE 4: Predicted;
KW ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Biotin {ECO:0000256|ARBA:ARBA00023267};
KW Hydrolase {ECO:0000256|ARBA:ARBA00022801};
KW Ligase {ECO:0000256|ARBA:ARBA00022598};
KW Lyase {ECO:0000313|EMBL:BAP45472.1};
KW Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW ProRule:PRU00409}; Reference proteome {ECO:0000313|Proteomes:UP000031652}.
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..1204
FT /note="Lipoyl-binding"
FT /evidence="ECO:0000259|PROSITE:PS50968"
SQ SEQUENCE 1209 AA; 131449 MW; E83B3580CA327724 CRC64;
MFNTVLIANR GEIAVRAIRT LKRLGIKSVA VYADADRNAA HVRDADVAIA LGGDKPADSY
LRIDKILAAA KQTGAQAIYP GYGFLSESAE FADACEQAGI AFVGPTAGQI REFGLKHRAR
ELAGQAQVPM APGTGLLDSL EQAVQAAEQI GYPVMLKTTA GGGGIGLTRC ADEPALRSAY
DSVKRMGEQF FSDAGVFLER FVDKARHVEV QIFGDGQGQV VALGERDCSL QRRNQKVVEE
TPAPNLPQAT RERLHAAAVQ LGQSVAYRSA GTVEFIYDPA RDDFYFLEVN TRLQVEHPIT
EMVTGLDLIE CMLQVAAGSP LDWAALRRAP QGAAIEVRLY AEDPLKNFQP SPGVLTDVYF
PDDVRVDGWV STGSEVSAFY DPMIAKLIVR GEDRADAMAR MQAALAATRL HGIASNLDYL
RQVVADPRFA RGDVWTRLLD DFTFKASVIE VLEPGTYSSV QDYPGRLGYW DIGVPPSGPM
DDQAFRLANR IVGNHVSAAA LEFTLQGPTL RFHSAALIAL TGADCPATLD GEPVAYWQPV
SVQAGQVLKL GRAQSGCRTY LAVRNGLDVP LYLGSRSTFA LGQFGGHAGR TLRTADMLAI
SQPELAACTT PAPISAPQAV HASLIPHYGN EWEIGVLYGP HGAPDFFTAQ SIEAFFAAEW
EVHYNSNRLG VRLSGPKPDW ARSDGGEAGL HPSNVHDCEY AIGAINFTGD FPVILTKDGP
SLGGFVCPVT IAKAELWKIG QVKPGDKLRF KPIGFQQAQS LEQAQLGSLE ALAAISAVPL
PAPALQPADT ASATILAELP ASGSRPRAVY RQAGDAYILL EYGDNVLDLA LRLRVHLLME
ALKARPLKGL EELAPGVRSL QLRYDSRVLH QKSLLEHLLM LEEGLGDVSQ LKVPTRIIHL
PMAFEDSATL GAVQRYRETV RSEAPWLPNN VDFLQRINGL DSREQVRDIL FQASYLILGL
GDVYLDAPCA VPLDPRHRLL SSKYNPARTF TAEGTVGIGG MYMCIYGMDS PGGYQLVGRT
LPIWNKYVKN PQFANGQPWL LHFFDQVRFY PVSEAELNEQ REAFREGRGQ IRIEHSEFDF
AEYQRLLADN AESIAEFQSR QKAAFDSEAQ LWHDDEPPVL RAAADSEADA QDYEGHLVSA
EMCGSVWKVL VEPGQHVEAG TPLLVVEAMK MELSVIAPVS GVVKAVRCQP GKAITPGDAL
VWLEPGEAA
//
