SPUC_PSEAE
ID SPUC_PSEAE Reviewed; 456 AA.
AC Q9I6J2;
DT 22-NOV-2017, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 110.
DE RecName: Full=Putrescine--pyruvate aminotransferase {ECO:0000303|PubMed:12081945};
DE Short=PATase {ECO:0000303|PubMed:12081945};
DE EC=2.6.1.113 {ECO:0000305|PubMed:12081945};
DE AltName: Full=Putrescine--pyruvate transaminase {ECO:0000305};
GN Name=spuC {ECO:0000303|PubMed:12081945};
GN OrderedLocusNames=PA0299 {ECO:0000312|EMBL:AAG03688.1};
OS Pseudomonas aeruginosa (strain ATCC 15692 / DSM 22644 / CIP 104116 / JCM
OS 14847 / LMG 12228 / 1C / PRS 101 / PAO1).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Pseudomonadales;
OC Pseudomonadaceae; Pseudomonas.
OX NCBI_TaxID=208964;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1 {ECO:0000312|Proteomes:UP000002438};
RX PubMed=10984043; DOI=10.1038/35023079;
RA Stover C.K., Pham X.-Q.T., Erwin A.L., Mizoguchi S.D., Warrener P.,
RA Hickey M.J., Brinkman F.S.L., Hufnagle W.O., Kowalik D.J., Lagrou M.,
RA Garber R.L., Goltry L., Tolentino E., Westbrock-Wadman S., Yuan Y.,
RA Brody L.L., Coulter S.N., Folger K.R., Kas A., Larbig K., Lim R.M.,
RA Smith K.A., Spencer D.H., Wong G.K.-S., Wu Z., Paulsen I.T., Reizer J.,
RA Saier M.H. Jr., Hancock R.E.W., Lory S., Olson M.V.;
RT "Complete genome sequence of Pseudomonas aeruginosa PAO1, an opportunistic
RT pathogen.";
RL Nature 406:959-964(2000).
RN [2]
RP FUNCTION, CATALYTIC ACTIVITY, DISRUPTION PHENOTYPE, INDUCTION, AND PATHWAY.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=12081945; DOI=10.1128/jb.184.14.3765-3773.2002;
RA Lu C.D., Itoh Y., Nakada Y., Jiang Y.;
RT "Functional analysis, and regulation of the divergent spuABCDEFGH-spuI
RT operons for polyamine uptake and utilization in Pseudomonas aeruginosa
RT PAO1.";
RL J. Bacteriol. 184:3765-3773(2002).
RN [3]
RP FUNCTION.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=18192388; DOI=10.1128/jb.01804-07;
RA Chou H.T., Kwon D.H., Hegazy M., Lu C.D.;
RT "Transcriptome analysis of agmatine and putrescine catabolism in
RT Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 190:1966-1975(2008).
CC -!- FUNCTION: Involved in the putrescine catabolism. Catalyzes the transfer
CC of the amino group from putrescine to pyruvate to yield 4-aminobutanal
CC and alanine. {ECO:0000269|PubMed:12081945,
CC ECO:0000269|PubMed:18192388}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=putrescine + pyruvate = 4-aminobutanal + L-alanine;
CC Xref=Rhea:RHEA:30707, ChEBI:CHEBI:15361, ChEBI:CHEBI:57972,
CC ChEBI:CHEBI:58264, ChEBI:CHEBI:326268; EC=2.6.1.113;
CC Evidence={ECO:0000305|PubMed:12081945};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000250|UniProtKB:P53555};
CC -!- PATHWAY: Amine and polyamine degradation; putrescine degradation; 4-
CC aminobutanal from putrescine (transaminase route).
CC {ECO:0000305|PubMed:12081945}.
CC -!- INDUCTION: By putrescine and agmatine. Also regulated by the global
CC CbrA/CbrB two-component system. {ECO:0000269|PubMed:12081945}.
CC -!- DISRUPTION PHENOTYPE: Cells lacking this gene are unable to utilize
CC putrescine as the sole source of carbon and nitrogen.
CC {ECO:0000269|PubMed:12081945}.
CC -!- SIMILARITY: Belongs to the class-III pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG03688.1; -; Genomic_DNA.
DR PIR; E83609; E83609.
DR RefSeq; NP_248990.1; NC_002516.2.
DR RefSeq; WP_003084297.1; NZ_QZGE01000016.1.
DR AlphaFoldDB; Q9I6J2; -.
DR SMR; Q9I6J2; -.
DR STRING; 287.DR97_3261; -.
DR PaxDb; Q9I6J2; -.
DR PRIDE; Q9I6J2; -.
DR EnsemblBacteria; AAG03688; AAG03688; PA0299.
DR GeneID; 878357; -.
DR KEGG; pae:PA0299; -.
DR PATRIC; fig|208964.12.peg.313; -.
DR PseudoCAP; PA0299; -.
DR HOGENOM; CLU_016922_4_1_6; -.
DR InParanoid; Q9I6J2; -.
DR OMA; IHPYTNL; -.
DR PhylomeDB; Q9I6J2; -.
DR BioCyc; MetaCyc:MON-17; -.
DR BioCyc; PAER208964:G1FZ6-301-MON; -.
DR BRENDA; 2.6.1.113; 5087.
DR BRENDA; 2.6.1.29; 5087.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0003867; F:4-aminobutyrate transaminase activity; IBA:GO_Central.
DR GO; GO:0004015; F:adenosylmethionine-8-amino-7-oxononanoate transaminase activity; IBA:GO_Central.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IEA:InterPro.
DR GO; GO:0008483; F:transaminase activity; IMP:PseudoCAP.
DR GO; GO:0009102; P:biotin biosynthetic process; IBA:GO_Central.
DR GO; GO:0009448; P:gamma-aminobutyric acid metabolic process; IBA:GO_Central.
DR GO; GO:0009447; P:putrescine catabolic process; IMP:PseudoCAP.
DR CDD; cd00610; OAT_like; 1.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR005814; Aminotrans_3.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00202; Aminotran_3; 1.
DR PIRSF; PIRSF000521; Transaminase_4ab_Lys_Orn; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00600; AA_TRANSFER_CLASS_3; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Pyridoxal phosphate; Reference proteome; Transferase.
FT CHAIN 1..456
FT /note="Putrescine--pyruvate aminotransferase"
FT /id="PRO_0000442298"
FT BINDING 156
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 262
FT /ligand="pyridoxal 5'-phosphate"
FT /ligand_id="ChEBI:CHEBI:597326"
FT /evidence="ECO:0000250|UniProtKB:P12995"
FT BINDING 322
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT BINDING 417
FT /ligand="substrate"
FT /evidence="ECO:0000250|UniProtKB:P53555"
FT MOD_RES 291
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250|UniProtKB:P53555"
SQ SEQUENCE 456 AA; 50453 MW; 01493131BE1683B8 CRC64;
MNSQITNAKT REWQALSRDH HLPPFTDYKQ LNEKGARIIT KAEGVYIWDS EGNKILDAMA
GLWCVNVGYG REELVQAATR QMRELPFYNL FFQTAHPPVV ELAKAIADVA PEGMNHVFFT
GSGSEANDTV LRMVRHYWAT KGQPQKKVVI GRWNGYHGST VAGVSLGGMK ALHEQGDFPI
PGIVHIAQPY WYGEGGDMSP DEFGVWAAEQ LEKKILEVGE ENVAAFIAEP IQGAGGVIVP
PDTYWPKIRE ILAKYDILFI ADEVICGFGR TGEWFGSQYY GNAPDLMPIA KGLTSGYIPM
GGVVVRDEIV EVLNQGGEFY HGFTYSGHPV AAAVALENIR ILREEKIIEK VKAETAPYLQ
KRWQELADHP LVGEARGVGM VAALELVKNK KTRERFTDKG VGMLCREHCF RNGLIMRAVG
DTMIISPPLV IDPSQIDELI TLARKCLDQT AAAVLA
