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Database: UniProt
Entry: V9TRP8_9PROT
LinkDB: V9TRP8_9PROT
Original site: V9TRP8_9PROT 
ID   V9TRP8_9PROT            Unreviewed;       472 AA.
AC   V9TRP8;
DT   19-MAR-2014, integrated into UniProtKB/TrEMBL.
DT   19-MAR-2014, sequence version 1.
DT   27-MAR-2024, entry version 44.
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:AHC73584.1};
GN   ORFNames=P856_363 {ECO:0000313|EMBL:AHC73584.1};
OS   Candidatus Endolissoclinum faulkneri L5.
OC   Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodospirillales;
OC   Rhodospirillaceae; Endolissoclinum.
OX   NCBI_TaxID=1401328 {ECO:0000313|EMBL:AHC73584.1, ECO:0000313|Proteomes:UP000018700};
RN   [1] {ECO:0000313|EMBL:AHC73584.1, ECO:0000313|Proteomes:UP000018700}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=faulkneri L5 {ECO:0000313|Proteomes:UP000018700};
RX   PubMed=24324632;
RA   Kwan J.C., Schmidt E.W.;
RT   "Bacterial endosymbiosis in a chordate host: long-term co-evolution and
RT   conservation of secondary metabolism.";
RL   PLoS ONE 8:E80822-E80822(2013).
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}.
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DR   EMBL; CP006745; AHC73584.1; -; Genomic_DNA.
DR   AlphaFoldDB; V9TRP8; -.
DR   STRING; 1401328.P856_363; -.
DR   KEGG; efk:P856_363; -.
DR   PATRIC; fig|1401328.3.peg.352; -.
DR   eggNOG; COG0165; Bacteria.
DR   HOGENOM; CLU_027272_2_3_5; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000018700; Chromosome.
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|ARBA:ARBA00023239, ECO:0000256|HAMAP-Rule:MF_00006};
KW   Reference proteome {ECO:0000313|Proteomes:UP000018700}.
FT   DOMAIN          18..310
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          374..443
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   472 AA;  52808 MW;  99DBDA2AD4C9FCCE CRC64;
     MMLSMTKTAA IDSMRGGRFV DVIEDAVARI NTSIDFDRRL WREDIAGSKA HVEMLVAQRI
     ITKEDGYVIE RALGEIWSEI DSGTFNFLHS LEDIHLNIEH RLHEKIGDTA GRLHTGRSRN
     DQIALDMKLW IRGVVDLIDS ELKELQAVLI ERADQYAETI MPGFTHLQPA QPITFGHHLM
     AYVEMLGRDR TRLADARRRM NENPLGAAAL AGTQFPIDRQ MTSAILGFDR PAANSLDAVS
     DRDFVMEVLA SAGICAVHLS RLAEELIIWT TSQFSFVHLS DSLTTGSSIM PQKKNPDGAE
     LVKGKTGRIL SAFTIIAIVL KGMPLSYGKD MQEDKEPCFD AIDNLRLCIA CTTSIVRNLQ
     ANQEAMRKAV FASFVTATDL ADWLVRETKM PFRNAHYIVG QVVRVAEEKC CGLADLPLDL
     LRKIHHAFDE RVYKILSIDA SLNARSSYGG TAPVRVREQI IEARKRFLGR SC
//
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