ASTB_MYXXD
ID ASTB_MYXXD Reviewed; 440 AA.
AC Q1DDF6;
DT 28-NOV-2006, integrated into UniProtKB/Swiss-Prot.
DT 11-JUL-2006, sequence version 1.
DT 03-AUG-2022, entry version 97.
DE RecName: Full=N-succinylarginine dihydrolase {ECO:0000255|HAMAP-Rule:MF_01172};
DE EC=3.5.3.23 {ECO:0000255|HAMAP-Rule:MF_01172};
GN Name=astB {ECO:0000255|HAMAP-Rule:MF_01172}; OrderedLocusNames=MXAN_1056;
OS Myxococcus xanthus (strain DK1622).
OC Bacteria; Proteobacteria; Deltaproteobacteria; Myxococcales;
OC Cystobacterineae; Myxococcaceae; Myxococcus.
OX NCBI_TaxID=246197;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DK1622;
RX PubMed=17015832; DOI=10.1073/pnas.0607335103;
RA Goldman B.S., Nierman W.C., Kaiser D., Slater S.C., Durkin A.S., Eisen J.,
RA Ronning C.M., Barbazuk W.B., Blanchard M., Field C., Halling C., Hinkle G.,
RA Iartchuk O., Kim H.S., Mackenzie C., Madupu R., Miller N., Shvartsbeyn A.,
RA Sullivan S.A., Vaudin M., Wiegand R., Kaplan H.B.;
RT "Evolution of sensory complexity recorded in a myxobacterial genome.";
RL Proc. Natl. Acad. Sci. U.S.A. 103:15200-15205(2006).
CC -!- FUNCTION: Catalyzes the hydrolysis of N(2)-succinylarginine into N(2)-
CC succinylornithine, ammonia and CO(2). {ECO:0000255|HAMAP-
CC Rule:MF_01172}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2 H(+) + 2 H2O + N(2)-succinyl-L-arginine = CO2 + N(2)-
CC succinyl-L-ornithine + 2 NH4(+); Xref=Rhea:RHEA:19533,
CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:16526,
CC ChEBI:CHEBI:28938, ChEBI:CHEBI:58241, ChEBI:CHEBI:58514; EC=3.5.3.23;
CC Evidence={ECO:0000255|HAMAP-Rule:MF_01172};
CC -!- PATHWAY: Amino-acid degradation; L-arginine degradation via AST
CC pathway; L-glutamate and succinate from L-arginine: step 2/5.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SUBUNIT: Homodimer. {ECO:0000255|HAMAP-Rule:MF_01172}.
CC -!- SIMILARITY: Belongs to the succinylarginine dihydrolase family.
CC {ECO:0000255|HAMAP-Rule:MF_01172}.
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DR EMBL; CP000113; ABF87851.1; -; Genomic_DNA.
DR RefSeq; WP_011551177.1; NC_008095.1.
DR AlphaFoldDB; Q1DDF6; -.
DR SMR; Q1DDF6; -.
DR STRING; 246197.MXAN_1056; -.
DR EnsemblBacteria; ABF87851; ABF87851; MXAN_1056.
DR GeneID; 41358509; -.
DR KEGG; mxa:MXAN_1056; -.
DR eggNOG; COG3724; Bacteria.
DR HOGENOM; CLU_053835_0_0_7; -.
DR OMA; TLNDWVD; -.
DR OrthoDB; 567590at2; -.
DR UniPathway; UPA00185; UER00280.
DR Proteomes; UP000002402; Chromosome.
DR GO; GO:0009015; F:N-succinylarginine dihydrolase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0019544; P:arginine catabolic process to glutamate; IEA:UniProtKB-UniRule.
DR GO; GO:0019545; P:arginine catabolic process to succinate; IEA:UniProtKB-UniPathway.
DR Gene3D; 3.75.10.20; -; 1.
DR HAMAP; MF_01172; AstB; 1.
DR InterPro; IPR037031; AstB_sf.
DR InterPro; IPR007079; SuccinylArg_d-Hdrlase_AstB.
DR Pfam; PF04996; AstB; 1.
DR TIGRFAMs; TIGR03241; arg_catab_astB; 1.
PE 3: Inferred from homology;
KW Arginine metabolism; Hydrolase; Reference proteome.
FT CHAIN 1..440
FT /note="N-succinylarginine dihydrolase"
FT /id="PRO_0000262358"
FT REGION 17..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 172
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 246
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT ACT_SITE 364
FT /note="Nucleophile"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 17..26
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 108
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 135..136
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 210
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 248
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
FT BINDING 358
FT /ligand="substrate"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01172"
SQ SEQUENCE 440 AA; 48058 MW; F52B6766873B98DA CRC64;
MREYNFDGLV GPTHNYGGLS PGNLASQSHV GEPSHPRDAA LQGLEKMRFV SALGVGQAVL
PPQPRPSLHA LRALGFTGSD EEVITRAARE AEHLLRLTSS ASSMWTANAA TVAPSADTAD
GRVHLTPANL SQMYHRAIEA ETTHSVLRAI FSNEKYFAVH APLPGSGHFA DEGAANHTRL
ATPGHAGVHL LAWGRSAWQD VQGPSRFPAR QTLEASQALA RLHQLDAKSV LFPQQHPEGI
DAGAFHTDVL AVGNERFLML HELAFVDHAG LLAVLREKLG QDFRAVVATK AELPAKDAVK
AYPFNSQVLT LPDGTMAIVA PIESRETPAA RQFLERVVAE DTPVKAVHYL DVRQSMNNGG
GPACLRQRVW LTDEERGAIK ADVFYTPALH DSLAGWVRRH YREVLRPKDL QDPQLARETM
TALDELTRIL NLGSVYDFQR
