ID U4KHH4_9VIBR Unreviewed; 624 AA.
AC U4KHH4;
DT 11-DEC-2013, integrated into UniProtKB/TrEMBL.
DT 11-DEC-2013, sequence version 1.
DT 27-MAR-2024, entry version 51.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argHA {ECO:0000313|EMBL:CCO59564.1};
GN Synonyms=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN ORFNames=VIBNI_A3591 {ECO:0000313|EMBL:CCO59564.1};
OS Vibrio nigripulchritudo.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC Vibrio.
OX NCBI_TaxID=28173 {ECO:0000313|EMBL:CCO59564.1, ECO:0000313|Proteomes:UP000016895};
RN [1] {ECO:0000313|EMBL:CCO59564.1, ECO:0000313|Proteomes:UP000016895}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=SnF1 {ECO:0000313|Proteomes:UP000016895};
RX PubMed=23739050; DOI=10.1038/ismej.2013.90;
RA Goudenege D., Labreuche Y., Krin E., Ansquer D., Mangenot S., Calteau A.,
RA Medigue C., Mazel D., Polz M.F., Le Roux F.;
RT "Comparative genomics of pathogenic lineages of Vibrio nigripulchritudo
RT identifies virulence-associated traits.";
RL ISME J. 7:1985-1996(2013).
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 Evidence={ECO:0000256|ARBA:ARBA00000985, ECO:0000256|HAMAP-
CC Rule:MF_00006, ECO:0000256|PIRNR:PIRNR036456};
CC -!- PATHWAY: Amino-acid biosynthesis; L-arginine biosynthesis; L-arginine
CC from L-ornithine and carbamoyl phosphate: step 3/3.
CC {ECO:0000256|ARBA:ARBA00004941, ECO:0000256|HAMAP-Rule:MF_00006,
CC ECO:0000256|PIRNR:PIRNR036456}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006,
CC ECO:0000256|PIRNR:PIRNR036456}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000256|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: In the N-terminal section; belongs to the lyase 1 family.
CC Argininosuccinate lyase subfamily. {ECO:0000256|ARBA:ARBA00005552,
CC ECO:0000256|PIRNR:PIRNR036456}.
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; FO203526; CCO59564.1; -; Genomic_DNA.
DR RefSeq; WP_004405346.1; NZ_JXXT01000013.1.
DR AlphaFoldDB; U4KHH4; -.
DR STRING; 28173.VIBNI_A3591; -.
DR KEGG; vni:VIBNI_A3591; -.
DR PATRIC; fig|1260221.3.peg.3410; -.
DR eggNOG; COG0165; Bacteria.
DR eggNOG; COG1246; Bacteria.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000016895; 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:UniProtKB-UniRule.
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 {ECO:0000256|ARBA:ARBA00023315,
KW ECO:0000256|PIRNR:PIRNR036456};
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006,
KW ECO:0000256|PIRNR:PIRNR036456};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006};
KW Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|PIRNR:PIRNR036456};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000256|PIRNR:PIRNR036456};
KW Reference proteome {ECO:0000313|Proteomes:UP000016895};
KW Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036456}.
FT DOMAIN 464..598
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 624 AA; 69085 MW; 99422107DCE799AA CRC64;
MALWGGRFTQ AADTRFKQFN DSLRFDYRLA EQDIVGSIAW SKALLSVGVL SEGEQQKLEL
ALNELKLEVM ENPEKILRSD AEDIHSWVEQ QLIGKVGDLG KKLHTGRSRN DQVATDLKLW
CRQQGHQLLM ALDRLQGQMV EVAKEHQGTV LPGYTHLQRA QPVTFAHWCL AYVEMFERDY
SRLSDAIKRL DTCPLGSGAL AGTAYPMDRE KLAHSLGFRR ATRNSLDSVS DRDHVMELMS
VASISMLHLS RLAEDMIFYN SGESNFIELA DTVTSGSSLM PQKKNPDALE LIRGKCGRVY
GSMAGMMMTV KALPLAYNKD MQEDKEGLFD ALDTWNECME MAALCFDGIK VNGERTLEAA
KQGYANSTEL ADYLVAKDIP FREAHHIVGV AVVAAIAKGC ALEELSISEL KEFSEVIEED
VYDILTIESC LEKRSALGGV SPTQVAYAVD QAQQRLSQRD ASGVKVRAAR LTDIDALDGM
VAYWAGLGEN LPRNRNELVR DIGSFAVAEH QGEVTGCGSL YVYDSGLAEI RTLGVEAGWQ
GQGQGSAIVA HLVEKARQMA IKKVFVLTRV PEFFMKYNFI PTSKSLLPEK VLKDCDQCPR
THACDEVALE INLAEQVITK ASVA
//
