ID A0A2T4JYU9_9RHOB Unreviewed; 476 AA.
AC A0A2T4JYU9;
DT 18-JUL-2018, integrated into UniProtKB/TrEMBL.
DT 18-JUL-2018, sequence version 1.
DT 24-JAN-2024, entry version 15.
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:PTE23078.1};
GN ORFNames=C5F48_03865 {ECO:0000313|EMBL:PTE23078.1};
OS Cereibacter changlensis JA139.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Cereibacter.
OX NCBI_TaxID=1188249 {ECO:0000313|EMBL:PTE23078.1, ECO:0000313|Proteomes:UP000241010};
RN [1] {ECO:0000313|EMBL:PTE23078.1, ECO:0000313|Proteomes:UP000241010}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=JA139 {ECO:0000313|EMBL:PTE23078.1,
RC ECO:0000313|Proteomes:UP000241010};
RA Meyer T.E., Miller S., Lodha T., Gandham S., Chintalapati S.,
RA Chintalapati V.R.;
RT "Cereibacter changlensis.";
RL Submitted (MAR-2018) 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 -!- 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 -!- 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:PTE23078.1}.
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DR EMBL; PZKG01000010; PTE23078.1; -; Genomic_DNA.
DR AlphaFoldDB; A0A2T4JYU9; -.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000241010; 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:PTE23078.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000241010}.
FT DOMAIN 20..314
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 377..445
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 476 AA; 51522 MW; ACE43B801C6E0E07 CRC64;
MTASPKSPDA ATQANAMWGG RFAAGPDAIM QAINASIGFD QRLYAQDIQG SRAHAAMLAA
QGILTNKDAE AIGEGLLTVL SEIETGAFPF RVELEDIHMN VEARLKEIIG EPAGRLHTAR
SRNDQVAVDF RLWVRDQCDA AITGIEALIA AFLAQAEAGA DWVMPGFTHL QTAQPVTWGH
HMLAYVEMLG RDRSRFVDAR DRMNECPLGA AALAGTGFPI DREMTARALG FDRPTANSLD
SVSDRDFALE FLSASSICAL HLSRFAEELV IWSSAQFRFV RLSDKWTTGS SIMPQKKNPD
AAELLRSKIG RILGATVALF TVMKGLPLTY SKDMQEDKEQ VFDAADTLML GLAAMTGMVQ
DMTANRDSLA AAAASGFSTA TDLADWLVRE LDLPFREAHH ITGALVAEAE AQGCDLPDLT
LEQMQAVHAG IRANVFEVLG VENSIRSRTS YGGTAPDNVR AQVARWKTAL STPEKP
//