AAMHY_RHILO
ID AAMHY_RHILO Reviewed; 278 AA.
AC Q988D4;
DT 01-OCT-2014, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2001, sequence version 1.
DT 03-AUG-2022, entry version 107.
DE RecName: Full=2-(acetamidomethylene)succinate hydrolase;
DE EC=3.5.1.29;
DE AltName: Full=alpha-(N-acetylaminomethylene)succinic acid amidohydrolase;
DE Short=AAMS amidohydrolase;
GN OrderedLocusNames=mlr6787;
OS Mesorhizobium japonicum (strain LMG 29417 / CECT 9101 / MAFF 303099)
OS (Mesorhizobium loti (strain MAFF 303099)).
OC Bacteria; Proteobacteria; Alphaproteobacteria; Hyphomicrobiales;
OC Phyllobacteriaceae; Mesorhizobium.
OX NCBI_TaxID=266835;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=11214968; DOI=10.1093/dnares/7.6.331;
RA Kaneko T., Nakamura Y., Sato S., Asamizu E., Kato T., Sasamoto S.,
RA Watanabe A., Idesawa K., Ishikawa A., Kawashima K., Kimura T., Kishida Y.,
RA Kiyokawa C., Kohara M., Matsumoto M., Matsuno A., Mochizuki Y.,
RA Nakayama S., Nakazaki N., Shimpo S., Sugimoto M., Takeuchi C., Yamada M.,
RA Tabata S.;
RT "Complete genome structure of the nitrogen-fixing symbiotic bacterium
RT Mesorhizobium loti.";
RL DNA Res. 7:331-338(2000).
RN [2]
RP PROTEIN SEQUENCE OF 1-10, FUNCTION, CATALYTIC ACTIVITY, SUBUNIT,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND PATHWAY.
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=18635903; DOI=10.3177/jnsv.54.185;
RA Yuan B., Yokochi N., Yoshikane Y., Ohnishi K., Ge F., Yagi T.;
RT "Gene identification and characterization of the pyridoxine degradative
RT enzyme alpha-(N-acetylaminomethylene)succinic acid amidohydrolase from
RT Mesorhizobium loti MAFF303099.";
RL J. Nutr. Sci. Vitaminol. 54:185-190(2008).
RN [3]
RP IDENTIFICATION.
RX PubMed=24826896; DOI=10.1371/journal.pone.0097250;
RA Shearer A.G., Altman T., Rhee C.D.;
RT "Finding sequences for over 270 orphan enzymes.";
RL PLoS ONE 9:E97250-E97250(2014).
RN [4]
RP X-RAY CRYSTALLOGRAPHY (2.26 ANGSTROMS) IN COMPLEX WITH CHLORIDE, SUBUNIT,
RP ACTIVE SITE, AND MUTAGENESIS OF SER-106; ASP-130 AND SER-230.
RC STRAIN=LMG 29417 / CECT 9101 / MAFF 303099;
RX PubMed=20099871; DOI=10.1021/bi901812p;
RA McCulloch K.M., Mukherjee T., Begley T.P., Ealick S.E.;
RT "Structure determination and characterization of the vitamin B6 degradative
RT enzyme (E)-2-(acetamidomethylene)succinate hydrolase.";
RL Biochemistry 49:1226-1235(2010).
CC -!- FUNCTION: Catalyzes the final reaction in the degradation of vitamin B6
CC from (E)-2-(acetamidomethylene)succinate (E-2AMS) to produce succinic
CC semialdehyde, acetate, ammonia and carbon dioxide.
CC {ECO:0000269|PubMed:18635903}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(acetamidomethylene)succinate + H(+) + 2 H2O = acetate + CO2
CC + NH4(+) + succinate semialdehyde; Xref=Rhea:RHEA:10432,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:30089, ChEBI:CHEBI:57698,
CC ChEBI:CHEBI:57706; EC=3.5.1.29;
CC Evidence={ECO:0000269|PubMed:18635903};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=53.7 uM for 2-(acetamidomethylene)succinate
CC {ECO:0000269|PubMed:18635903};
CC Note=kcat is 307.3 min(-1) for 2-(acetamidomethylene)succinate.;
CC pH dependence:
CC Optimum pH is 7.0. {ECO:0000269|PubMed:18635903};
CC -!- PATHWAY: Cofactor degradation; B6 vitamer degradation.
CC {ECO:0000269|PubMed:18635903}.
CC -!- SUBUNIT: Homodimer. {ECO:0000269|PubMed:18635903,
CC ECO:0000269|PubMed:20099871}.
CC -!- SIMILARITY: Belongs to the AB hydrolase superfamily. {ECO:0000305}.
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DR EMBL; BA000012; BAB53016.1; -; Genomic_DNA.
DR RefSeq; WP_010914326.1; NC_002678.2.
DR PDB; 3KXP; X-ray; 2.26 A; A/B/C/D/E/F/G/H/I/J/K/L=1-278.
DR PDBsum; 3KXP; -.
DR AlphaFoldDB; Q988D4; -.
DR SMR; Q988D4; -.
DR STRING; 266835.14026419; -.
DR ESTHER; meslo-MLR6787; 6_AlphaBeta_hydrolase.
DR EnsemblBacteria; BAB53016; BAB53016; BAB53016.
DR KEGG; mlo:mlr6787; -.
DR eggNOG; COG0596; Bacteria.
DR eggNOG; COG2945; Bacteria.
DR HOGENOM; CLU_020336_50_4_5; -.
DR OMA; RRSHWPD; -.
DR OrthoDB; 1439833at2; -.
DR BioCyc; MetaCyc:MON-20510; -.
DR BRENDA; 3.5.1.29; 12422.
DR UniPathway; UPA00192; -.
DR EvolutionaryTrace; Q988D4; -.
DR Proteomes; UP000000552; Chromosome.
DR GO; GO:0047411; F:2-(acetamidomethylene)succinate hydrolase activity; IDA:UniProtKB.
DR GO; GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
DR GO; GO:0042820; P:vitamin B6 catabolic process; IDA:UniProtKB.
DR Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR000073; AB_hydrolase_1.
DR Pfam; PF12697; Abhydrolase_6; 1.
DR PRINTS; PR00111; ABHYDROLASE.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Chloride; Direct protein sequencing; Hydrolase.
FT CHAIN 1..278
FT /note="2-(acetamidomethylene)succinate hydrolase"
FT /id="PRO_0000430445"
FT ACT_SITE 106
FT /note="Nucleophile"
FT /evidence="ECO:0000305|PubMed:20099871"
FT ACT_SITE 130
FT /evidence="ECO:0000305|PubMed:20099871"
FT ACT_SITE 258
FT /evidence="ECO:0000305|PubMed:20099871"
FT BINDING 41
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT /evidence="ECO:0000269|PubMed:20099871"
FT BINDING 106..107
FT /ligand="chloride"
FT /ligand_id="ChEBI:CHEBI:17996"
FT MUTAGEN 106
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:20099871"
FT MUTAGEN 130
FT /note="D->N: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:20099871"
FT MUTAGEN 230
FT /note="S->A: Loss of catalytic activity."
FT /evidence="ECO:0000269|PubMed:20099871"
FT STRAND 13..18
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 23..29
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 32..38
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 45..48
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 49..53
FT /evidence="ECO:0007829|PDB:3KXP"
FT TURN 54..58
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 59..64
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 81..95
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 100..105
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 107..118
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 120..122
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 137..146
FT /evidence="ECO:0007829|PDB:3KXP"
FT TURN 147..150
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 154..156
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 157..167
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 173..182
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 183..187
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 190..195
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 197..206
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 212..217
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 222..227
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 231..233
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 235..244
FT /evidence="ECO:0007829|PDB:3KXP"
FT STRAND 250..253
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 260..263
FT /evidence="ECO:0007829|PDB:3KXP"
FT HELIX 265..277
FT /evidence="ECO:0007829|PDB:3KXP"
SQ SEQUENCE 278 AA; 29896 MW; 675601C06DF3EA12 CRC64;
MDMAADIASD HFISRRVDIG RITLNVREKG SGPLMLFFHG ITSNSAVFEP LMIRLSDRFT
TIAVDQRGHG LSDKPETGYE ANDYADDIAG LIRTLARGHA ILVGHSLGAR NSVTAAAKYP
DLVRSVVAID FTPYIETEAL DALEARVNAG SQLFEDIKAV EAYLAGRYPN IPADAIRIRA
ESGYQPVDGG LRPLASSAAM AQTARGLRSD LVPAYRDVTK PVLIVRGESS KLVSAAALAK
TSRLRPDLPV VVVPGADHYV NEVSPEITLK AITNFIDA
