ID B5JSZ5_9GAMM Unreviewed; 467 AA.
AC B5JSZ5;
DT 14-OCT-2008, integrated into UniProtKB/TrEMBL.
DT 14-OCT-2008, sequence version 1.
DT 24-JAN-2024, entry version 68.
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 ECO:0000313|EMBL:EDY87200.1};
GN ORFNames=GP5015_2378 {ECO:0000313|EMBL:EDY87200.1};
OS gamma proteobacterium HTCC5015.
OC Bacteria; Pseudomonadota; Gammaproteobacteria.
OX NCBI_TaxID=391615 {ECO:0000313|EMBL:EDY87200.1, ECO:0000313|Proteomes:UP000004692};
RN [1] {ECO:0000313|Proteomes:UP000004692}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=HTCC5015 {ECO:0000313|Proteomes:UP000004692};
RX PubMed=20472792; DOI=10.1128/JB.00510-10;
RA Thrash J.C., Stingl U., Cho J.C., Ferriera S., Johnson J., Vergin K.L.,
RA Giovannoni S.J.;
RT "Genome sequence of the novel marine member of the Gammaproteobacteria
RT strain HTCC5015.";
RL J. Bacteriol. 192:3838-3839(2010).
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006}.
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}.
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DR EMBL; DS990599; EDY87200.1; -; Genomic_DNA.
DR AlphaFoldDB; B5JSZ5; -.
DR STRING; 391615.GP5015_2378; -.
DR eggNOG; COG0165; Bacteria.
DR HOGENOM; CLU_027272_2_3_6; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000004692; Unassembled WGS sequence.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
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 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; IPR029419; Arg_succ_lyase_C.
DR InterPro; IPR009049; Argininosuccinate_lyase.
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; IPR008948; L-Aspartase-like.
DR NCBIfam; TIGR00838; argH; 1.
DR PANTHER; PTHR43814; ARGININOSUCCINATE LYASE; 1.
DR PANTHER; PTHR43814:SF1; ARGININOSUCCINATE LYASE; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00145; ARGSUCLYASE.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; L-aspartase-like; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 3: Inferred from homology;
KW Amino-acid biosynthesis {ECO:0000256|HAMAP-Rule:MF_00006};
KW Arginine biosynthesis {ECO:0000256|ARBA:ARBA00022571, ECO:0000256|HAMAP-
KW Rule:MF_00006}; Cytoplasm {ECO:0000256|HAMAP-Rule:MF_00006};
KW Lyase {ECO:0000256|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:EDY87200.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000004692}.
FT DOMAIN 17..311
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 374..442
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 467 AA; 51782 MW; 086ED895D869BB42 CRC64;
MTDQRLQDDQ GYKPWGGRFS EPTDAFVEAF TASIQFDQRL YRHDIAGSRA HARMLGHVGV
LDSAEVDAIL NGLDEIEADI ERGGVEWSIS LEDVHMNIEA RLTDKIGIAG KKLHTGRSRN
DQVATDIRLY LRDEIDAILV EVERLLRGLL ELAEKNADTI MPGFTHLQVA QPVTFGHHLM
AWFEMLKRDR ARLLDCRKRV NVLPLGAAAL AGTTYPIDRE FVARELGFDS VAENSLDAVS
DRDFAIEFCA AAALAMTHLT RWSEELVLWS SAQFAFIKLP DRFCTGSSIM PQKKNPDVPE
LVRGKVGRVN GHLISLLTLM KSQPLAYNKD NQEDKEPLFD AIDTLRGSMR AFADMVPHLE
ARADNMRKAA KQGFSTATDL ADYLVRKGIP FRDAHEVVGN AVAWCEEANC DLADMPLVEL
QNFCDGIGED VFEVLTLEGS VAARDHIGGT APAQVRAAVE RARASLA
//
