ID A0A0A0EMU5_9RHOB Unreviewed; 463 AA.
AC A0A0A0EMU5;
DT 07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT 07-JAN-2015, sequence version 1.
DT 24-JAN-2024, entry version 41.
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=ATO9_03245 {ECO:0000313|EMBL:KGM50517.1};
OS Pseudooceanicola atlanticus.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Paracoccaceae; Pseudooceanicola.
OX NCBI_TaxID=1461694 {ECO:0000313|EMBL:KGM50517.1, ECO:0000313|Proteomes:UP000030004};
RN [1] {ECO:0000313|EMBL:KGM50517.1, ECO:0000313|Proteomes:UP000030004}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=22II-s11g {ECO:0000313|EMBL:KGM50517.1,
RC ECO:0000313|Proteomes:UP000030004};
RX PubMed=25663028; DOI=10.1007/s10482-015-0398-2;
RA Lai Q., Li G., Liu X., Du Y., Sun F., Shao Z.;
RT "Pseudooceanicola atlanticus gen. nov. sp. nov., isolated from surface
RT seawater of the Atlantic Ocean and reclassification of Oceanicola
RT batsensis, Oceanicola marinus, Oceanicola nitratireducens, Oceanicola
RT nanhaiensis, Oceanicola antarcticus and Oceanicola flagellatus, as
RT Pseudooceanicola batsensis comb. nov., Pseudooceanicola marinus comb. nov.,
RT Pseudooceanicola nitratireducens comb. nov., Pseudooceanicola nanhaiensis
RT comb. nov., Pseudooceanicola antarcticus comb. nov., and Pseudooceanicola
RT flagellatus comb. nov.";
RL Antonie Van Leeuwenhoek 107:1065-1074(2015).
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:KGM50517.1}.
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DR EMBL; AQQX01000001; KGM50517.1; -; Genomic_DNA.
DR RefSeq; WP_043744888.1; NZ_CP051248.1.
DR AlphaFoldDB; A0A0A0EMU5; -.
DR STRING; 1461694.ATO9_03245; -.
DR eggNOG; COG0165; Bacteria.
DR OrthoDB; 9769623at2; -.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000030004; 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:KGM50517.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000030004}.
FT DOMAIN 12..306
FT /note="Fumarate lyase N-terminal"
FT /evidence="ECO:0000259|Pfam:PF00206"
FT DOMAIN 369..438
FT /note="Argininosuccinate lyase C-terminal"
FT /evidence="ECO:0000259|Pfam:PF14698"
SQ SEQUENCE 463 AA; 50300 MW; 57A41B33F0FE5DDF CRC64;
MTDKNANQMW GGRFAAGPDA IMEAINASIG FDQRMAAQDI AGSRAHAAML AATGIVSDKD
AEAMREGLLT ILSEIEEGKF VFSTALEDIH MNVEARLKDL IGDPAGRLHT GRSRNDQVAT
DFKLWTRDQM DAAIEGLQAL MRALLEQAEQ GADWVMPGFT HLQTAQPVTW GHHMMAYVEM
LGRDLSRFRD ARARMNESPL GAAALAGTSY PIDRDMTAQA LGFDRPAANS LDAVSDRDFA
LEFLSCASIC AMHLSRFAEE LVIWSSAQFR FVTLSDRFST GSSIMPQKKN PDAAELIRAK
IGRIFGANVA LMTVMKGLPL AYSKDMQEDK EQVFDAADNL MLALAAMTGM VSDMTANRPA
LEAAAAHGFS TATDLADWLV RVLDMPFREA HHVTGSLVAK AEAKGCDLPD LSLDEMQAVH
SAITEDVFTV LGVHNSVASR TSYGGTAPVR VREQVGRWKE ALA
//