HPXW_KLEP7
ID HPXW_KLEP7 Reviewed; 528 AA.
AC A6T9C8;
DT 20-DEC-2017, integrated into UniProtKB/Swiss-Prot.
DT 21-AUG-2007, sequence version 1.
DT 03-AUG-2022, entry version 74.
DE RecName: Full=Oxamate amidohydrolase proenzyme {ECO:0000303|PubMed:27303801};
DE EC=3.5.1.126 {ECO:0000269|PubMed:27303801};
DE Contains:
DE RecName: Full=Oxamate amidohydrolase large chain {ECO:0000305};
DE AltName: Full=Oxamate amidohydrolase alpha chain {ECO:0000303|PubMed:27303801};
DE Contains:
DE RecName: Full=Oxamate amidohydrolase small chain {ECO:0000305};
DE AltName: Full=Oxamate amidohydrolase beta chain {ECO:0000303|PubMed:27303801};
DE Flags: Precursor;
GN Name=hpxW {ECO:0000303|PubMed:27303801};
GN ORFNames=KPN_01768 {ECO:0000312|EMBL:ABR77199.1};
OS Klebsiella pneumoniae subsp. pneumoniae (strain ATCC 700721 / MGH 78578).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Klebsiella/Raoultella group; Klebsiella.
OX NCBI_TaxID=272620;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 700721 / MGH 78578 {ECO:0000312|Proteomes:UP000000265};
RG The Klebsiella pneumonia Genome Sequencing Project;
RA McClelland M., Sanderson E.K., Spieth J., Clifton W.S., Latreille P.,
RA Sabo A., Pepin K., Bhonagiri V., Porwollik S., Ali J., Wilson R.K.;
RL Submitted (SEP-2006) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP X-RAY CRYSTALLOGRAPHY (2.65 ANGSTROMS) OF 1-341 AND 342-528, FUNCTION,
RP CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, AUTOCATALYTIC CLEAVAGE,
RP ACTIVE SITE, MUTAGENESIS OF THR-342 AND SER-360, REACTION MECHANISM, AND
RP SUBUNIT.
RX PubMed=27303801; DOI=10.1107/s2059798316007099;
RA Hicks K.A., Ealick S.E.;
RT "Biochemical and structural characterization of Klebsiella pneumoniae
RT oxamate amidohydrolase in the uric acid degradation pathway.";
RL Acta Crystallogr. D 72:808-816(2016).
CC -!- FUNCTION: Involved in the uric acid degradation pathway. Catalyzes the
CC conversion of oxamate to oxalate. {ECO:0000269|PubMed:27303801}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=H2O + oxamate = NH4(+) + oxalate; Xref=Rhea:RHEA:51512,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:28938, ChEBI:CHEBI:30623,
CC ChEBI:CHEBI:58363; EC=3.5.1.126;
CC Evidence={ECO:0000269|PubMed:27303801};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC Note=kcat is 5.5 sec(-1) with oxamate as substrate.
CC {ECO:0000269|PubMed:27303801};
CC -!- SUBUNIT: Heterodimer that consists of a 35.5 kDa large (alpha) subunit
CC and a 20 kDa small (beta) subunit, which are synthesized from a single
CC polypeptide. {ECO:0000269|PubMed:27303801}.
CC -!- PTM: Cleaved by autocatalysis into a large (alpha) and a small (beta)
CC subunit. {ECO:0000269|PubMed:27303801}.
CC -!- SIMILARITY: Belongs to the gamma-glutamyltransferase family.
CC {ECO:0000305}.
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; CP000647; ABR77199.1; -; Genomic_DNA.
DR RefSeq; WP_015958435.1; NC_009648.1.
DR PDB; 5HFT; X-ray; 2.65 A; A/C=1-341, B/D=342-528.
DR PDBsum; 5HFT; -.
DR AlphaFoldDB; A6T9C8; -.
DR SMR; A6T9C8; -.
DR STRING; 272620.KPN_01768; -.
DR MEROPS; T03.025; -.
DR EnsemblBacteria; ABR77199; ABR77199; KPN_01768.
DR KEGG; kpn:KPN_01768; -.
DR HOGENOM; CLU_014813_3_0_6; -.
DR OMA; GCKLAMA; -.
DR BRENDA; 3.5.1.126; 2817.
DR Proteomes; UP000000265; Chromosome.
DR GO; GO:0008233; F:peptidase activity; IEA:UniProtKB-KW.
DR GO; GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
DR Gene3D; 1.10.246.130; -; 1.
DR Gene3D; 3.60.20.40; -; 1.
DR InterPro; IPR043138; GGT_lsub_C.
DR InterPro; IPR043137; GGT_ssub.
DR InterPro; IPR029055; Ntn_hydrolases_N.
DR SUPFAM; SSF56235; SSF56235; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Hydrolase; Protease; Reference proteome; Zymogen.
FT CHAIN 1..341
FT /note="Oxamate amidohydrolase large chain"
FT /id="PRO_0000442767"
FT CHAIN 342..528
FT /note="Oxamate amidohydrolase small chain"
FT /id="PRO_0000442768"
FT ACT_SITE 342
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:27303801"
FT BINDING 424..425
FT /ligand="substrate"
FT /evidence="ECO:0000305|PubMed:27303801"
FT SITE 360
FT /note="Important for catalytic activity"
FT /evidence="ECO:0000305|PubMed:27303801"
FT MUTAGEN 342
FT /note="T->A: Unable to autoprocess into a mature
FT heterodimer. Lack of amidohydrolase activity."
FT /evidence="ECO:0000269|PubMed:27303801"
FT MUTAGEN 360
FT /note="S->A: Forms a heterodimer, however lacks
FT amidohydrolase activity."
FT /evidence="ECO:0000269|PubMed:27303801"
FT STRAND 5..16
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 17..28
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 33..47
FT /evidence="ECO:0007829|PDB:5HFT"
FT TURN 49..51
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 56..63
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 65..67
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 70..74
FT /evidence="ECO:0007829|PDB:5HFT"
FT TURN 84..89
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 95..97
FT /evidence="ECO:0007829|PDB:5HFT"
FT TURN 98..100
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 107..121
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 128..131
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 133..141
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 147..155
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 157..160
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 166..170
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 181..183
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 186..198
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 202..205
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 207..219
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 225..229
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 239..243
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 246..250
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 254..264
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 278..282
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 286..295
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 315..318
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 343..348
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 354..360
FT /evidence="ECO:0007829|PDB:5HFT"
FT TURN 364..367
FT /evidence="ECO:0007829|PDB:5HFT"
FT TURN 372..374
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 382..384
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 408..412
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 417..423
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 429..442
FT /evidence="ECO:0007829|PDB:5HFT"
FT HELIX 446..451
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 501..507
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 513..516
FT /evidence="ECO:0007829|PDB:5HFT"
FT TURN 519..522
FT /evidence="ECO:0007829|PDB:5HFT"
FT STRAND 524..528
FT /evidence="ECO:0007829|PDB:5HFT"
SQ SEQUENCE 528 AA; 55542 MW; 5375362CBACF6316 CRC64;
MHSSNVSTHG MAVAPHHLAS QSALAILREG GSAIEAMVAA AAAIAVVYPH MNGLGGDGFW
LIVPPEGDPI AIDASGAAGS LATLEAYAGQ RHIPNRGPQA ALTVAGTVSG WVEALRISRD
LTGRALPVAR LLADAIGYAE DGIPVTASQA HATASKLEEL RHQPGFSETW LVAGEAPRPG
SRFRQPALAG TLRMLASDGL DSFYRGPLAE RLAQGMAALG MPITLGDLQA HRARRPGPLT
LQHQQGTLWN LAPPTQGLVS LAILGITDRL KMADADDAQT VHRIVEATKR AFALRDAHIT
DPRHLDVDVQ QLLTPEALQP LADSIDDASA SPWGGGKGPG DTVWMGVVDN SGLAVSFIQS
IYHEFGSGVV LPDTGIVWQN RGAAFSLDPQ HLLALAPGKQ PFHTLNPAAA RLNDGRVMVY
GSMGGDGQPQ TQAALFTRYI LQGVPLQESI SRPRWLLGRT WGQSSDSLKL EGRFAPACIA
RLRELGHDVE VLADFSEAMG HAGAIVRHPN GLLEGATDPR SNGAAAGY
