ARLY_MYCTU
ID ARLY_MYCTU Reviewed; 470 AA.
AC P9WPY7; L0TA28; P0A4Z0; P94994;
DT 16-APR-2014, integrated into UniProtKB/Swiss-Prot.
DT 16-APR-2014, sequence version 1.
DT 03-AUG-2022, entry version 43.
DE RecName: Full=Argininosuccinate lyase {ECO:0000255|HAMAP-Rule:MF_00006};
DE Short=ASAL {ECO:0000255|HAMAP-Rule:MF_00006};
DE EC=4.3.2.1 {ECO:0000255|HAMAP-Rule:MF_00006};
DE AltName: Full=Arginosuccinase {ECO:0000255|HAMAP-Rule:MF_00006};
GN Name=argH {ECO:0000255|HAMAP-Rule:MF_00006}; OrderedLocusNames=Rv1659;
GN ORFNames=MTCY06H11.24;
OS Mycobacterium tuberculosis (strain ATCC 25618 / H37Rv).
OC Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC Mycobacterium; Mycobacterium tuberculosis complex.
OX NCBI_TaxID=83332;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=9634230; DOI=10.1038/31159;
RA Cole S.T., Brosch R., Parkhill J., Garnier T., Churcher C.M., Harris D.E.,
RA Gordon S.V., Eiglmeier K., Gas S., Barry C.E. III, Tekaia F., Badcock K.,
RA Basham D., Brown D., Chillingworth T., Connor R., Davies R.M., Devlin K.,
RA Feltwell T., Gentles S., Hamlin N., Holroyd S., Hornsby T., Jagels K.,
RA Krogh A., McLean J., Moule S., Murphy L.D., Oliver S., Osborne J.,
RA Quail M.A., Rajandream M.A., Rogers J., Rutter S., Seeger K., Skelton S.,
RA Squares S., Squares R., Sulston J.E., Taylor K., Whitehead S.,
RA Barrell B.G.;
RT "Deciphering the biology of Mycobacterium tuberculosis from the complete
RT genome sequence.";
RL Nature 393:537-544(1998).
RN [2]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC STRAIN=ATCC 25618 / H37Rv;
RX PubMed=21969609; DOI=10.1074/mcp.m111.011627;
RA Kelkar D.S., Kumar D., Kumar P., Balakrishnan L., Muthusamy B., Yadav A.K.,
RA Shrivastava P., Marimuthu A., Anand S., Sundaram H., Kingsbury R.,
RA Harsha H.C., Nair B., Prasad T.S., Chauhan D.S., Katoch K., Katoch V.M.,
RA Kumar P., Chaerkady R., Ramachandran S., Dash D., Pandey A.;
RT "Proteogenomic analysis of Mycobacterium tuberculosis by high resolution
RT mass spectrometry.";
RL Mol. Cell. Proteomics 10:M111.011627-M111.011627(2011).
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; Evidence={ECO:0000255|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. {ECO:0000255|HAMAP-
CC Rule:MF_00006}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000255|HAMAP-Rule:MF_00006}.
CC -!- SIMILARITY: Belongs to the lyase 1 family. Argininosuccinate lyase
CC subfamily. {ECO:0000255|HAMAP-Rule:MF_00006}.
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DR EMBL; AL123456; CCP44424.1; -; Genomic_DNA.
DR PIR; F70621; F70621.
DR RefSeq; NP_216175.1; NC_000962.3.
DR RefSeq; WP_003408180.1; NZ_NVQJ01000069.1.
DR PDB; 6IEM; X-ray; 2.20 A; A/B/C/D/E/F/G/H=1-470.
DR PDB; 6IEN; X-ray; 2.70 A; A/B/C/D=1-470.
DR PDB; 6IG5; X-ray; 2.08 A; A/B/C/D=1-470.
DR PDB; 6IGA; X-ray; 2.78 A; A/B/C/D=1-470.
DR PDBsum; 6IEM; -.
DR PDBsum; 6IEN; -.
DR PDBsum; 6IG5; -.
DR PDBsum; 6IGA; -.
DR AlphaFoldDB; P9WPY7; -.
DR SMR; P9WPY7; -.
DR STRING; 83332.Rv1659; -.
DR PaxDb; P9WPY7; -.
DR DNASU; 885365; -.
DR GeneID; 885365; -.
DR KEGG; mtu:Rv1659; -.
DR TubercuList; Rv1659; -.
DR eggNOG; COG0165; Bacteria.
DR OMA; KKNPDVF; -.
DR PhylomeDB; P9WPY7; -.
DR BRENDA; 4.3.2.1; 3445.
DR UniPathway; UPA00068; UER00114.
DR Proteomes; UP000001584; Chromosome.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0009274; C:peptidoglycan-based cell wall; HDA:MTBBASE.
DR GO; GO:0004056; F:argininosuccinate lyase activity; IBA:GO_Central.
DR GO; GO:0042450; P:arginine biosynthetic process via ornithine; IBA:GO_Central.
DR CDD; cd01359; Argininosuccinate_lyase; 1.
DR Gene3D; 1.10.275.10; -; 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 PANTHER; PTHR43814; PTHR43814; 1.
DR Pfam; PF14698; ASL_C2; 1.
DR Pfam; PF00206; Lyase_1; 1.
DR PRINTS; PR00149; FUMRATELYASE.
DR SUPFAM; SSF48557; SSF48557; 1.
DR TIGRFAMs; TIGR00838; argH; 1.
DR PROSITE; PS00163; FUMARATE_LYASES; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Amino-acid biosynthesis; Arginine biosynthesis; Cytoplasm;
KW Lyase; Reference proteome.
FT CHAIN 1..470
FT /note="Argininosuccinate lyase"
FT /id="PRO_0000137793"
FT HELIX 19..25
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 28..31
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 32..34
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 35..51
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 57..75
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 88..106
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 107..109
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 115..150
FT /evidence="ECO:0007829|PDB:6IG5"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:6IG5"
FT STRAND 163..169
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 170..175
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 178..195
FT /evidence="ECO:0007829|PDB:6IG5"
FT TURN 203..206
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 214..221
FT /evidence="ECO:0007829|PDB:6IG5"
FT STRAND 224..226
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 230..235
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 238..265
FT /evidence="ECO:0007829|PDB:6IG5"
FT TURN 267..269
FT /evidence="ECO:0007829|PDB:6IG5"
FT STRAND 271..273
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 276..278
FT /evidence="ECO:0007829|PDB:6IG5"
FT STRAND 279..281
FT /evidence="ECO:0007829|PDB:6IG5"
FT STRAND 283..285
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 292..315
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 324..329
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 330..352
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 358..364
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 367..370
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 371..381
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 386..403
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 407..409
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 412..418
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 424..429
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 432..437
FT /evidence="ECO:0007829|PDB:6IG5"
FT HELIX 447..468
FT /evidence="ECO:0007829|PDB:6IG5"
SQ SEQUENCE 470 AA; 49774 MW; 1844ED923D797ECE CRC64;
MSTNEGSLWG GRFAGGPSDA LAALSKSTHF DWVLAPYDLT ASRAHTMVLF RAGLLTEEQR
DGLLAGLDSL AQDVADGSFG PLVTDEDVHA ALERGLIDRV GPDLGGRLRA GRSRNDQVAA
LFRMWLRDAV RRVATGVLDV VGALAEQAAA HPSAIMPGKT HLQSAQPILL AHHLLAHAHP
LLRDLDRIVD FDKRAAVSPY GSGALAGSSL GLDPDAIAAD LGFSAAADNS VDATAARDFA
AEAAFVFAMI AVDLSRLAED IIVWSSTEFG YVTLHDSWST GSSIMPQKKN PDIAELARGK
SGRLIGNLAG LLATLKAQPL AYNRDLQEDK EPVFDSVAQL ELLLPAMAGL VASLTFNVQR
MAELAPAGYT LATDLAEWLV RQGVPFRSAH EAAGAAVRAA EQRGVGLQEL TDDELAAISP
ELTPQVREVL TIEGSVSARD CRGGTAPGRV AEQLNAIGEA AERLRRQLVR
