ARUH_PSEAE
ID ARUH_PSEAE Reviewed; 393 AA.
AC Q9HUI9;
DT 05-SEP-2012, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Arginine--pyruvate transaminase AruH;
DE EC=2.6.1.84;
GN Name=aruH; OrderedLocusNames=PA4976;
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;
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 PATHWAY, INDUCTION, AND GENE NAME.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17416670; DOI=10.1128/jb.00261-07;
RA Yang Z., Lu C.D.;
RT "Functional genomics enables identification of genes of the arginine
RT transaminase pathway in Pseudomonas aeruginosa.";
RL J. Bacteriol. 189:3945-3953(2007).
RN [3]
RP FUNCTION, CATALYTIC ACTIVITY, COFACTOR, BIOPHYSICOCHEMICAL PROPERTIES,
RP PATHWAY, AND SUBUNIT.
RC STRAIN=ATCC 15692 / DSM 22644 / CIP 104116 / JCM 14847 / LMG 12228 / 1C /
RC PRS 101 / PAO1;
RX PubMed=17416668; DOI=10.1128/jb.00262-07;
RA Yang Z., Lu C.D.;
RT "Characterization of an arginine:pyruvate transaminase in arginine
RT catabolism of Pseudomonas aeruginosa PAO1.";
RL J. Bacteriol. 189:3954-3959(2007).
CC -!- FUNCTION: Catalyzes the conversion of L-arginine into 2-ketoarginine
CC via transamination. L-arginine is the best substrate, but it can also
CC use L-lysine, L-methionine, L-leucine, ornithine and L-glutamine, which
CC indicates that it may have a broader physiological function in amino
CC acid catabolism. {ECO:0000269|PubMed:17416668}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=L-arginine + pyruvate = 5-guanidino-2-oxopentanoate + L-
CC alanine; Xref=Rhea:RHEA:13833, ChEBI:CHEBI:15361, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57972, ChEBI:CHEBI:58489; EC=2.6.1.84;
CC Evidence={ECO:0000269|PubMed:17416668};
CC -!- COFACTOR:
CC Name=pyridoxal 5'-phosphate; Xref=ChEBI:CHEBI:597326;
CC Evidence={ECO:0000269|PubMed:17416668};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=1.6 mM for pyruvate {ECO:0000269|PubMed:17416668};
CC KM=13.9 mM for L-arginine {ECO:0000269|PubMed:17416668};
CC Vmax=54.6 umol/min/mg enzyme {ECO:0000269|PubMed:17416668};
CC Note=kcat is 38.6 sec(-1).;
CC pH dependence:
CC Optimum pH is 9.0. {ECO:0000269|PubMed:17416668};
CC Temperature dependence:
CC Optimum temperature is 42 degrees Celsius.
CC {ECO:0000269|PubMed:17416668};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation.
CC {ECO:0000269|PubMed:17416668, ECO:0000269|PubMed:17416670}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:17416668}.
CC -!- INDUCTION: Induced by L-arginine in the absence of ArgR, via the
CC AruR/AruS two-component regulatory system.
CC {ECO:0000269|PubMed:17416670}.
CC -!- SIMILARITY: Belongs to the class-I pyridoxal-phosphate-dependent
CC aminotransferase family. {ECO:0000305}.
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DR EMBL; AE004091; AAG08361.1; -; Genomic_DNA.
DR PIR; F83024; F83024.
DR RefSeq; NP_253663.1; NC_002516.2.
DR RefSeq; WP_003102073.1; NZ_QZGE01000002.1.
DR AlphaFoldDB; Q9HUI9; -.
DR SMR; Q9HUI9; -.
DR STRING; 287.DR97_2329; -.
DR PaxDb; Q9HUI9; -.
DR EnsemblBacteria; AAG08361; AAG08361; PA4976.
DR GeneID; 880915; -.
DR KEGG; pae:PA4976; -.
DR PATRIC; fig|208964.12.peg.5212; -.
DR PseudoCAP; PA4976; -.
DR HOGENOM; CLU_017584_4_0_6; -.
DR InParanoid; Q9HUI9; -.
DR OMA; CAGMIGR; -.
DR PhylomeDB; Q9HUI9; -.
DR BioCyc; PAER208964:G1FZ6-5092-MON; -.
DR BRENDA; 2.6.1.84; 5087.
DR UniPathway; UPA00073; -.
DR Proteomes; UP000002438; Chromosome.
DR GO; GO:0030170; F:pyridoxal phosphate binding; IDA:UniProtKB.
DR GO; GO:0008483; F:transaminase activity; IDA:UniProtKB.
DR GO; GO:0006527; P:arginine catabolic process; IDA:PseudoCAP.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IMP:UniProtKB.
DR GO; GO:0009058; P:biosynthetic process; IEA:InterPro.
DR Gene3D; 3.40.640.10; -; 1.
DR Gene3D; 3.90.1150.10; -; 1.
DR InterPro; IPR004839; Aminotransferase_I/II.
DR InterPro; IPR004838; NHTrfase_class1_PyrdxlP-BS.
DR InterPro; IPR015424; PyrdxlP-dep_Trfase.
DR InterPro; IPR015421; PyrdxlP-dep_Trfase_major.
DR InterPro; IPR015422; PyrdxlP-dep_Trfase_small.
DR Pfam; PF00155; Aminotran_1_2; 1.
DR SUPFAM; SSF53383; SSF53383; 1.
DR PROSITE; PS00105; AA_TRANSFER_CLASS_1; 1.
PE 1: Evidence at protein level;
KW Aminotransferase; Arginine metabolism; Pyridoxal phosphate; Pyruvate;
KW Reference proteome; Transferase.
FT CHAIN 1..393
FT /note="Arginine--pyruvate transaminase AruH"
FT /id="PRO_0000418388"
FT MOD_RES 237
FT /note="N6-(pyridoxal phosphate)lysine"
FT /evidence="ECO:0000250"
SQ SEQUENCE 393 AA; 42380 MW; B28593585BAEC860 CRC64;
MRYSDFTQRI AGDGAAAWDI HYRALARVEQ GEEILLLSVG DPDFDTPAPI VQAAIDSLLA
GNTHYADVRG KRALRQRIAE RHRRRSGQAV DAEQVVVLAG AQCALYAVVQ CLLNPGDEVI
VAEPMYVTYE AVFGACGARV VPVPVRSENG FRVQAEEVAA LITPRTRAMA LNSPHNPSGA
SLPRATWEAL AELCMAHDLW MISDEVYSEL LFDGEHVSPA SLPGMADRTA TLNSLSKSHA
MTGWRVGWVV GPAALCAHLE NLALCMLYGS PEFIQDAACT ALEAPLPELE AMREAYRRRR
DLVIECLADS PGLRPLRPDG GMFVMVDIRP TGLSAQAFAD RLLDRHGVSV LAGEAFGPSA
AGHIRLGLVL GAEPLREACR RIALCAAELL GQA
