ID   GCS2_MYCPA              Reviewed;         376 AA.
AC   Q73T00;
DT   26-APR-2005, integrated into UniProtKB/Swiss-Prot.
DT   26-APR-2005, sequence version 2.
DT   25-MAY-2022, entry version 90.
DE   RecName: Full=Putative glutamate--cysteine ligase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            EC=6.3.2.2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE   AltName: Full=Gamma-glutamylcysteine synthetase 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
DE            Short=Gamma-GCS 2 {ECO:0000255|HAMAP-Rule:MF_01609};
GN   OrderedLocusNames=MAP_3922;
OS   Mycolicibacterium paratuberculosis (strain ATCC BAA-968 / K-10)
OS   (Mycobacterium paratuberculosis).
OC   Bacteria; Actinobacteria; Corynebacteriales; Mycobacteriaceae;
OC   Mycobacterium; Mycobacterium avium complex (MAC).
OX   NCBI_TaxID=262316;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=ATCC BAA-968 / K-10;
RX   PubMed=16116077; DOI=10.1073/pnas.0505662102;
RA   Li L., Bannantine J.P., Zhang Q., Amonsin A., May B.J., Alt D., Banerji N.,
RA   Kanjilal S., Kapur V.;
RT   "The complete genome sequence of Mycobacterium avium subspecies
RT   paratuberculosis.";
RL   Proc. Natl. Acad. Sci. U.S.A. 102:12344-12349(2005).
CC   -!- FUNCTION: ATP-dependent carboxylate-amine ligase which exhibits weak
CC       glutamate--cysteine ligase activity. {ECO:0000255|HAMAP-Rule:MF_01609}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=ATP + L-cysteine + L-glutamate = ADP + gamma-L-glutamyl-L-
CC         cysteine + H(+) + phosphate; Xref=Rhea:RHEA:13285, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:29985, ChEBI:CHEBI:30616, ChEBI:CHEBI:35235,
CC         ChEBI:CHEBI:43474, ChEBI:CHEBI:58173, ChEBI:CHEBI:456216; EC=6.3.2.2;
CC         Evidence={ECO:0000255|HAMAP-Rule:MF_01609};
CC   -!- SIMILARITY: Belongs to the glutamate--cysteine ligase type 2 family.
CC       YbdK subfamily. {ECO:0000255|HAMAP-Rule:MF_01609}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAS06472.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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DR   EMBL; AE016958; AAS06472.1; ALT_INIT; Genomic_DNA.
DR   RefSeq; WP_015632730.1; NC_002944.2.
DR   AlphaFoldDB; Q73T00; -.
DR   SMR; Q73T00; -.
DR   STRING; 262316.MAP_3922; -.
DR   EnsemblBacteria; AAS06472; AAS06472; MAP_3922.
DR   GeneID; 66695804; -.
DR   KEGG; mpa:MAP_3922; -.
DR   eggNOG; COG2170; Bacteria.
DR   HOGENOM; CLU_044848_1_0_11; -.
DR   OMA; LIFGLHV; -.
DR   Proteomes; UP000000580; Chromosome.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR   GO; GO:0004357; F:glutamate-cysteine ligase activity; IEA:UniProtKB-EC.
DR   GO; GO:0042398; P:cellular modified amino acid biosynthetic process; IEA:InterPro.
DR   HAMAP; MF_01609; Glu_cys_ligase_2; 1.
DR   InterPro; IPR006336; GCS2.
DR   InterPro; IPR014746; Gln_synth/guanido_kin_cat_dom.
DR   InterPro; IPR011793; YbdK.
DR   Pfam; PF04107; GCS2; 1.
DR   SUPFAM; SSF55931; SSF55931; 1.
DR   TIGRFAMs; TIGR02050; gshA_cyan_rel; 1.
PE   3: Inferred from homology;
KW   ATP-binding; Ligase; Nucleotide-binding; Reference proteome.
FT   CHAIN           1..376
FT                   /note="Putative glutamate--cysteine ligase 2"
FT                   /id="PRO_0000218207"
SQ   SEQUENCE   376 AA;  42552 MW;  C7089754BB14E87F CRC64;
     MPARRGDAHI DFARSPRPTI GVEWEFALVD AQTRDLSNEA TAVIAEIGEN PRVHKELLRN
     TVEVVSGICR TVPEAMEDLR QTLGPARRIV RDRGMELFCA GAHPFAQWTT QKLTDAPRYA
     ELIKRTQWWG RQMLIWGVHV HVGISSPNKV MPIMTSLLNY YPHLLALSAS SPWWTGVDTG
     YASNRAMMFQ QLPTAGLPFQ FQTWAEFEGF VYDQKKTGII DHVDEVRWDI RPSPHLGTLE
     MRICDGVSNL HELAALVALT HCLVVDLDRR LEADESLPTM PPWHHQENKW RAARYGLDAV
     IILDADSNER LVTEDLDDVL NRLEPVARKL QCADELAAVA DIPRHGASYQ RQRRVAEEHD
     GDLRAVVDAL VAELEI