ID   A0A151TX50_CAJCA        Unreviewed;       994 AA.
AC   A0A151TX50;
DT   08-JUN-2016, integrated into UniProtKB/TrEMBL.
DT   08-JUN-2016, sequence version 1.
DT   27-MAR-2024, entry version 20.
DE   SubName: Full=D-alanine--D-alanine ligase {ECO:0000313|EMBL:KYP71659.1};
GN   ORFNames=KK1_010929 {ECO:0000313|EMBL:KYP71659.1};
OS   Cajanus cajan (Pigeon pea) (Cajanus indicus).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Fabales; Fabaceae; Papilionoideae; 50 kb inversion clade;
OC   NPAAA clade; indigoferoid/millettioid clade; Phaseoleae; Cajanus.
OX   NCBI_TaxID=3821 {ECO:0000313|EMBL:KYP71659.1, ECO:0000313|Proteomes:UP000075243};
RN   [1] {ECO:0000313|EMBL:KYP71659.1, ECO:0000313|Proteomes:UP000075243}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=cv. Asha {ECO:0000313|Proteomes:UP000075243};
RX   PubMed=22057054; DOI=10.1038/nbt.2022;
RA   Varshney R.K., Chen W., Li Y., Bharti A.K., Saxena R.K., Schlueter J.A.,
RA   Donoghue M.T., Azam S., Fan G., Whaley A.M., Farmer A.D., Sheridan J.,
RA   Iwata A., Tuteja R., Penmetsa R.V., Wu W., Upadhyaya H.D., Yang S.P.,
RA   Shah T., Saxena K.B., Michael T., McCombie W.R., Yang B., Zhang G.,
RA   Yang H., Wang J., Spillane C., Cook D.R., May G.D., Xu X., Jackson S.A.;
RT   "Draft genome sequence of pigeonpea (Cajanus cajan), an orphan legume crop
RT   of resource-poor farmers.";
RL   Nat. Biotechnol. 30:83-89(2012).
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   EMBL; CM003605; KYP71659.1; -; Genomic_DNA.
DR   AlphaFoldDB; A0A151TX50; -.
DR   STRING; 3821.A0A151TX50; -.
DR   OMA; RQVAYHT; -.
DR   Proteomes; UP000075243; Chromosome 3.
DR   GO; GO:0005524; F:ATP binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0008716; F:D-alanine-D-alanine ligase activity; IEA:InterPro.
DR   GO; GO:0046872; F:metal ion binding; IEA:InterPro.
DR   GO; GO:0071555; P:cell wall organization; IEA:UniProtKB-KW.
DR   GO; GO:0008360; P:regulation of cell shape; IEA:UniProtKB-KW.
DR   Gene3D; 3.40.50.20; -; 2.
DR   Gene3D; 3.30.1490.20; ATP-grasp fold, A domain; 1.
DR   Gene3D; 3.30.470.20; ATP-grasp fold, B domain; 2.
DR   InterPro; IPR011761; ATP-grasp.
DR   InterPro; IPR013815; ATP_grasp_subdomain_1.
DR   InterPro; IPR000291; D-Ala_lig_Van_CS.
DR   InterPro; IPR011095; Dala_Dala_lig_C.
DR   InterPro; IPR011127; Dala_Dala_lig_N.
DR   InterPro; IPR016185; PreATP-grasp_dom_sf.
DR   PANTHER; PTHR23132; D-ALANINE--D-ALANINE LIGASE; 1.
DR   PANTHER; PTHR23132:SF0; D-ALANINE-D-ALANINE LIGASE FAMILY; 1.
DR   Pfam; PF07478; Dala_Dala_lig_C; 2.
DR   Pfam; PF01820; Dala_Dala_lig_N; 2.
DR   SUPFAM; SSF56059; Glutathione synthetase ATP-binding domain-like; 2.
DR   SUPFAM; SSF52440; PreATP-grasp domain; 2.
DR   PROSITE; PS50975; ATP_GRASP; 2.
DR   PROSITE; PS00843; DALA_DALA_LIGASE_1; 1.
DR   PROSITE; PS00844; DALA_DALA_LIGASE_2; 1.
PE   3: Inferred from homology;
KW   ATP-binding {ECO:0000256|ARBA:ARBA00022840, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Cell shape {ECO:0000256|ARBA:ARBA00022960};
KW   Cell wall biogenesis/degradation {ECO:0000256|ARBA:ARBA00023316};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Ligase {ECO:0000256|ARBA:ARBA00022598, ECO:0000313|EMBL:KYP71659.1};
KW   Nucleotide-binding {ECO:0000256|ARBA:ARBA00022741, ECO:0000256|PROSITE-
KW   ProRule:PRU00409}; Peptidoglycan synthesis {ECO:0000256|ARBA:ARBA00022984};
KW   Reference proteome {ECO:0000313|Proteomes:UP000075243}.
FT   DOMAIN          208..449
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          925..990
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   994 AA;  109090 MW;  7016B6BAD4E86AC4 CRC64;
     MATSSLAGAA SNFAVLRRTE TRSFSSSSPG GSVKLFRSAS TCRAARVSAL TRASSREVAV
     VGGGAAEKAK EKGRVLKVGL ICGGPSAERG ISLNSARSVL DHLQGDDLHV SCYYIDCNLN
     AYAISSAQVY SNTPNDFDFK LESLAQSFQT LDDLAKHLAT AVDIVFPVIH GQFGEDGGVQ
     ELLEKYNVPF VGTGSNECRQ AFDKHKASLE LRKLGFITVP SFLVQGHETN KSELSEWFIK
     HQIDPNSGKV VVKPTRGGSS IGVRVAYGVN DSLVKANEIM SEGIDNKVLI EIFLEGGSEF
     TAIVLDVGSG SDHCPVVLLP TEVELQFRGA NDVKENDAIF NYRRKYLPTQ QVAYHTPPRF
     PLDVIENIRK GASLLFQWLG LQDFARIDGW YLPNSGSKFS ASSESEFGRT ESGAIIFTDI
     NLISGMEQTS FLFQQASKVL LDVMMFCKHD TDHLNHFLFM HDCMDNSYRS LLEKAIYVIQ
     VGFSHTNILR SIIHHACLRF PNLASISRIS GQLPSRSKSL PLNKSFSLHE GARKVFVIFG
     GDTSERQVSL MSGTNVWLNL LAFHDLEVMP CLLSPTSECA SSADIGKKAD DVMNRTVWSL
     PYSLVLRHTT EEVLDACVEA IEPERAAITS NLRKKVMNDL MEGLKDHNWF TGFDIADDVP
     VKFSLRQWIK LAKEVQATVF IAVHGGIGED GTLQSLLDAE GVPYPGPGAM ASKTCMDKVA
     TSVALKHLAN SGVLTINKDV RKKADLFNKP VNDTWHDLTW KLQCQTLCVK PAKDGCSTGV
     ARLCCSEDLA IYVKALEDCL LRIPPNSLSK AHGMIEMPNP PPEHLIFEPF IETDEIIVTS
     KFEDSSGHGL TWKGHSRWVE ITVGVIGKRG SMYSLSPSVT VKESGDILSL EEKFQGGTGI
     NLTPPPLSIM SENALNRCKQ HIELIANTLQ LEGFSRIDAF VNVDSGEVLI IEVNTVPGMT
     PSTVLIHQAL VEQPPLYPHQ FFRKLLDLAS ERSM
//