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Database: UniProt
Entry: A0A2T4JYU9_9RHOB
LinkDB: A0A2T4JYU9_9RHOB
Original site: A0A2T4JYU9_9RHOB 
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
//
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