ID ARLY_VIBPA Reviewed; 624 AA.
AC P59620;
DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 23-APR-2003, sequence version 1.
DT 27-MAR-2024, entry version 125.
DE RecName: Full=Bifunctional protein ArgH;
DE Includes:
DE RecName: Full=Argininosuccinate lyase;
DE Short=ASAL;
DE EC=4.3.2.1;
DE AltName: Full=Arginosuccinase;
DE Includes:
DE RecName: Full=Probable acetyltransferase;
DE EC=2.3.1.-;
GN Name=argH; OrderedLocusNames=VP2756;
OS Vibrio parahaemolyticus serotype O3:K6 (strain RIMD 2210633).
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=223926;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=RIMD 2210633;
RX PubMed=12620739; DOI=10.1016/s0140-6736(03)12659-1;
RA Makino K., Oshima K., Kurokawa K., Yokoyama K., Uda T., Tagomori K.,
RA Iijima Y., Najima M., Nakano M., Yamashita A., Kubota Y., Kimura S.,
RA Yasunaga T., Honda T., Shinagawa H., Hattori M., Iida T.;
RT "Genome sequence of Vibrio parahaemolyticus: a pathogenic mechanism
RT distinct from that of V. cholerae.";
RL Lancet 361:743-749(2003).
CC -!- CATALYTIC ACTIVITY:
CC Reaction=2-(N(omega)-L-arginino)succinate = fumarate + L-arginine;
CC Xref=Rhea:RHEA:24020, ChEBI:CHEBI:29806, ChEBI:CHEBI:32682,
CC ChEBI:CHEBI:57472; EC=4.3.2.1;
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC Argininosuccinate lyase subfamily. {ECO:0000305}.
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DR EMBL; BA000031; BAC61019.1; -; Genomic_DNA.
DR RefSeq; NP_799135.1; NC_004603.1.
DR RefSeq; WP_005465154.1; NC_004603.1.
DR AlphaFoldDB; P59620; -.
DR SMR; P59620; -.
DR GeneID; 1190306; -.
DR KEGG; vpa:VP2756; -.
DR PATRIC; fig|223926.6.peg.2652; -.
DR eggNOG; COG0165; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR HOGENOM; CLU_027272_2_3_6; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000002493; Chromosome 1.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0016747; F:acyltransferase activity, transferring groups other than amino-acyl groups; IEA:InterPro.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IEA:UniProtKB-UniRule.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IEA:InterPro.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR CDD; cd04301; NAT_SF; 1.
DR Gene3D; 3.40.630.30; -; 1.
DR Gene3D; 1.10.40.30; Fumarase/aspartase (C-terminal domain); 1.
DR Gene3D; 1.20.200.10; Fumarase/aspartase (Central domain); 1.
DR Gene3D; 1.10.275.10; Fumarase/aspartase (N-terminal domain); 1.
DR HAMAP; MF_00006; Arg_succ_lyase; 1.
DR InterPro; IPR016181; Acyl_CoA_acyltransferase.
DR InterPro; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
DR InterPro; IPR011244; ASAL_AGS_AcTrfase.
DR InterPro; IPR024083; Fumarase/histidase_N.
DR InterPro; IPR020557; Fumarate_lyase_CS.
DR InterPro; IPR000362; Fumarate_lyase_fam.
DR InterPro; IPR022761; Fumarate_lyase_N.
DR InterPro; IPR000182; GNAT_dom.
DR InterPro; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF00583; Acetyltransf_1; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PIRSF; PIRSF036456; ASAL_AGS; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF55729; Acyl-CoA N-acyltransferases (Nat); 1.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
DR PROSITE; PS51186; GNAT; 1.
PE 3: Inferred from homology;
KW Acyltransferase; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Lyase; Multifunctional enzyme; Reference proteome; Transferase.
FT CHAIN 1..624
FT /note="Bifunctional protein ArgH"
FT /id="PRO_0000137847"
FT DOMAIN 464..614
FT /note="N-acetyltransferase"
FT REGION 1..466
FT /note="Argininosuccinate lyase"
FT REGION 467..624
FT /note="Probable acetyltransferase"
SQ SEQUENCE 624 AA; 69358 MW; DA5D4C815438ABCF CRC64;
MALWGGRFTQ AADTRFKEFN DSLRFDYRLA EQDIVGSIAW SKALLSVGVL SAEEQQKLEL
ALNELKLEVM EDPHQILRSD AEDIHSWVEQ QLISKVGDLG KKLHTGRSRN DQVATDLKLW
CRQQGQQLLI ALDRLQSQMV QVAKQHQGTV LPGYTHLQRA QPVTFAHWCL AYVEMFERDY
SRLSDALQRL DTCPLGSGAL AGTAYPIDRE QLAHNLGFHR ATRNSLDSVS DRDHVMELMS
VASISMLHLS RLAEDMIFYN SGESNFIELA DTVTSGSSLM PQKKNPDALE LIRGKTGRVY
GALAGMMMTV KALPLAYNKD MQEDKEGLFD ALDTWNDCME MAALCFDGIK VNGERTLEAA
KQGYANATEL ADYLVAKGIP FREAHHIVGV AVVGAIAKGC ALEELSLQEL QEFSDVIDND
VYDILTIESC LEKRSALGGV SPKQVAYAVD QADKRLAQRD SSAVKVRPAR LTDIETLEGM
VAYWANMGEN LPRSRNELVR DIGSFAVAEH HGEVTGCASL YVYDSGLAEI RSLGIEAGWQ
GQGQGSAIVN YLVDKARQMA IKKVFVLTRT PEFFMKQSFL PTSKSLLPEK VLKDCDQCPR
QHACDEVALE INLVEQIIQR SHVA
//
