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Database: UniProt
Entry: A0A0F5EXN3_AVIPA
LinkDB: A0A0F5EXN3_AVIPA
Original site: A0A0F5EXN3_AVIPA 
ID   A0A0F5EXN3_AVIPA        Unreviewed;       458 AA.
AC   A0A0F5EXN3;
DT   24-JUN-2015, integrated into UniProtKB/TrEMBL.
DT   24-JUN-2015, sequence version 1.
DT   27-MAR-2024, entry version 43.
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:QIR10847.1};
GN   ORFNames=EIG79_10350 {ECO:0000313|EMBL:RZN56406.1}, HBL79_00380
GN   {ECO:0000313|EMBL:QIR10847.1}, NCTC10926_02675
GN   {ECO:0000313|EMBL:SUV40625.1}, NCTC11296_02232
GN   {ECO:0000313|EMBL:STO72308.1};
OS   Avibacterium paragallinarum (Haemophilus gallinarum).
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Pasteurellales;
OC   Pasteurellaceae; Avibacterium.
OX   NCBI_TaxID=728 {ECO:0000313|EMBL:RZN56406.1, ECO:0000313|Proteomes:UP000294229};
RN   [1] {ECO:0000313|Proteomes:UP000254465, ECO:0000313|Proteomes:UP000254620}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=NCTC10926 {ECO:0000313|EMBL:SUV40625.1,
RC   ECO:0000313|Proteomes:UP000254620}, and NCTC11296
RC   {ECO:0000313|EMBL:STO72308.1, ECO:0000313|Proteomes:UP000254465};
RG   Pathogen Informatics;
RA   Doyle S.;
RL   Submitted (JUN-2018) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:RZN56406.1, ECO:0000313|Proteomes:UP000294229}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=SA-3 {ECO:0000313|EMBL:RZN56406.1,
RC   ECO:0000313|Proteomes:UP000294229};
RA   Hellmuth J.E., Boucher C.E., Cason E.D.;
RT   "Sequencing Av. paragallinarum serogroups.";
RL   Submitted (NOV-2018) to the EMBL/GenBank/DDBJ databases.
RN   [3] {ECO:0000313|EMBL:QIR10847.1, ECO:0000313|Proteomes:UP000503595}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ESV-135 {ECO:0000313|EMBL:QIR10847.1,
RC   ECO:0000313|Proteomes:UP000503595};
RA   Cobos-Justo M.E., Sanchez-Alonso M.P., Negrete-Abascal E., Perez V.,
RA   Soriano-Vargas E., Castelan H., Vazquez-Cruz C.;
RT   "Comparison of the genome sequence of three Mexican strains of Avibacterium
RT   paragallinarum.";
RL   Submitted (MAR-2020) 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   -!- 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; CP050316; QIR10847.1; -; Genomic_DNA.
DR   EMBL; RQXS01000067; RZN56406.1; -; Genomic_DNA.
DR   EMBL; UGHK01000002; STO72308.1; -; Genomic_DNA.
DR   EMBL; UFSW01000002; SUV40625.1; -; Genomic_DNA.
DR   RefSeq; WP_017805313.1; NZ_VXDA01000039.1.
DR   STRING; 728.VY92_02730; -.
DR   GeneID; 66255039; -.
DR   KEGG; apag:EIA51_02025; -.
DR   eggNOG; COG0165; Bacteria.
DR   OrthoDB; 9769623at2; -.
DR   UniPathway; UPA00068; UER00114.
DR   Proteomes; UP000254465; Unassembled WGS sequence.
DR   Proteomes; UP000254620; Unassembled WGS sequence.
DR   Proteomes; UP000294229; Unassembled WGS sequence.
DR   Proteomes; UP000503595; 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|HAMAP-Rule:MF_00006, ECO:0000313|EMBL:RZN56406.1}.
FT   DOMAIN          6..301
FT                   /note="Fumarate lyase N-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF00206"
FT   DOMAIN          364..431
FT                   /note="Argininosuccinate lyase C-terminal"
FT                   /evidence="ECO:0000259|Pfam:PF14698"
SQ   SEQUENCE   458 AA;  50982 MW;  739DB5322DD3B4C0 CRC64;
     MALWGGRFTQ AADKRFKDFN DSLRFDYRLA EQDIEGSIGW SKALVSVGVL TKAEQQQLEQ
     ALNELLIEVR SNLTGILQDD AEDIHSWVES KLINKVGNLG KKLHTGRSRN DQVALDIKMW
     CKQRVTELQY SIRALQRKLV ETAENNQHAV MPGYTHLQRA QPITFAHWCM AYVEMLDRDY
     SRLSDAYQRM NTCPLGSGAL AGTAYAIDRE ALAQDLGFAS ATRNSLDSVS DRDHIIELLS
     TASLSMAHLS RFAEDMIIFN SGEADFVELS DRVTSGSSLM PQKKNPDACE LIRGKAGRVV
     GALTGMLMTV KGLPLAYNKD MQEDKEGIFD ALDTWQDCLD MATFVLDDIK VNVDRTREAA
     LKGYSNATEL ADYLVAKGVP FRDSHHIVGE TVVYAISVHK GLEDLSLEEF RQFSDVVGDD
     IYAILSLQSC LDKRCAKGGV SPQRVAEAIA EAKVRLRS
//
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