ID A0A094IQJ7_9GAMM Unreviewed; 613 AA.
AC A0A094IQJ7;
DT 26-NOV-2014, integrated into UniProtKB/TrEMBL.
DT 26-NOV-2014, sequence version 1.
DT 27-MAR-2024, entry version 40.
DE RecName: Full=Argininosuccinate lyase {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000256|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000256|ARBA:ARBA00012338, ECO:0000256|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000256|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000256|HAMAP-Rule:MF_00006};
GN ORFNames=IDAT_03280 {ECO:0000313|EMBL:KFZ29392.1};
OS Pseudidiomarina atlantica.
OC Bacteria; Pseudomonadota; Gammaproteobacteria; Alteromonadales;
OC Idiomarinaceae; Pseudidiomarina.
OX NCBI_TaxID=1517416 {ECO:0000313|EMBL:KFZ29392.1, ECO:0000313|Proteomes:UP000053718};
RN [1] {ECO:0000313|EMBL:KFZ29392.1, ECO:0000313|Proteomes:UP000053718}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=MCCC 1A10513 {ECO:0000313|EMBL:KFZ29392.1,
RC ECO:0000313|Proteomes:UP000053718};
RA Du J., Lai Q., Shao Z.;
RT "Draft genome sequence of Idiomarina sp. MCCC 1A10513.";
RL Submitted (JUN-2014) to the EMBL/GenBank/DDBJ databases.
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};
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 -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC whole genome shotgun (WGS) entry which is preliminary data.
CC {ECO:0000313|EMBL:KFZ29392.1}.
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DR EMBL; JPIN01000002; KFZ29392.1; -; Genomic_DNA.
DR RefSeq; WP_034730446.1; NZ_JPIN01000002.1.
DR AlphaFoldDB; A0A094IQJ7; -.
DR STRING; 1517416.IDAT_03280; -.
DR eggNOG; COG0165; Bacteria.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000053718; Unassembled WGS sequence.
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 Transferase {ECO:0000256|ARBA:ARBA00022679, ECO:0000256|PIRNR:PIRNR036456}.
FT DOMAIN 464..602
FT /note="N-acetyltransferase"
FT /evidence="ECO:0000259|PROSITE:PS51186"
SQ SEQUENCE 613 AA; 67681 MW; B9D8483DB96EC018 CRC64;
MSLWGGRFSA PSAAEFKQFN DSLRFDYVLA PFDIQASQAW AKSLQQAGLL TSAEQQQLHD
ALGDLLKAVQ ANPELPLKSD AEDIHSWVEA QLIDKIGATA KRLHTGRSRN DLVATDLRLF
CKATCEQLIN ANLAAIQQLL LFAERYQAAP LPGYTHLQRA QPIMAGHWAL AYVQMLQRDV
SRLKEMRKRA DVCPLGSGAL AGTTAAIDRE ALAHELGFRF ASENSLDGVS DRDFALDILH
CAATGMLHLS RIAEDVIFYC SGESGCFAMS DRISSGSSLM PQKKNPDLFE LLRGKTGRVL
GQQHALQTTL KGLPLAYNKD MQEDKEGLFD ALQTYQQCLQ MLAFAMPELS VNEAHAKQQA
QLGYSNATEF ADYLVSKGMP FRDAHHVTGQ AVLFAQQQGQ PLEDLDIDTL RGFSDLIEPD
VYAFLELDYG LEQRRAIGGT APSAIKTALK HANDWLHAAE AASKHVRQAR LSDADKICEL
IAYWAAQGEN LPRDKADVLQ AIQSFAVAEI DDEVVGCAAL YVYSTGLAEI RSLGLFPQAQ
GKGMGAELVA FLLWKARELG ITRTIVLTRV PEFFGKLNFR LTVKDKLPEK VMKDCELCPR
KDNCDETALE YLL
//
