ID   A0A6J1DW40_MOMCH        Unreviewed;       957 AA.
AC   A0A6J1DW40;
DT   07-OCT-2020, integrated into UniProtKB/TrEMBL.
DT   07-OCT-2020, sequence version 1.
DT   28-JAN-2026, entry version 22.
DE   SubName: Full=Uncharacterized protein LOC111024031 {ECO:0000313|RefSeq:XP_022157299.1};
GN   Name=LOC111024031 {ECO:0000313|RefSeq:XP_022157299.1};
OS   Momordica charantia (Bitter gourd) (Balsam pear).
OC   Eukaryota; Viridiplantae; Streptophyta; Embryophyta; Tracheophyta;
OC   Spermatophyta; Magnoliopsida; eudicotyledons; Gunneridae; Pentapetalae;
OC   rosids; fabids; Cucurbitales; Cucurbitaceae; Momordiceae; Momordica.
OX   NCBI_TaxID=3673 {ECO:0000313|Proteomes:UP000504603, ECO:0000313|RefSeq:XP_022157299.1};
RN   [1] {ECO:0000313|RefSeq:XP_022157299.1}
RP   IDENTIFICATION.
RG   RefSeq;
RL   Submitted (AUG-2025) to UniProtKB.
CC   -!- SIMILARITY: Belongs to the D-alanine--D-alanine ligase family.
CC       {ECO:0000256|ARBA:ARBA00010871}.
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DR   RefSeq; XP_022157299.1; XM_022301607.1.
DR   AlphaFoldDB; A0A6J1DW40; -.
DR   GeneID; 111024031; -.
DR   KEGG; mcha:111024031; -.
DR   OrthoDB; 2013972at2759; -.
DR   Proteomes; UP000504603; Unplaced.
DR   GO; GO:0009507; C:chloroplast; IEA:TreeGrafter.
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   FunFam; 3.30.470.20:FF:000048; D-alanine--D-alanine ligase family; 1.
DR   FunFam; 3.30.470.20:FF:000061; D-alanine-D-alanine ligase family; 1.
DR   FunFam; 3.40.50.20:FF:000027; D-alanine-D-alanine ligase family; 1.
DR   FunFam; 3.40.50.20:FF:000028; D-alanine-D-alanine ligase family; 1.
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   Ligase {ECO:0000256|ARBA:ARBA00022598};
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:UP000504603}.
FT   DOMAIN          214..457
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
FT   DOMAIN          888..953
FT                   /note="ATP-grasp"
FT                   /evidence="ECO:0000259|PROSITE:PS50975"
SQ   SEQUENCE   957 AA;  105314 MW;  5B4647EB215A57B0 CRC64;
     MAYIANCSNC NVLSKTVKPR ASSFALTLSS SFLRSSVDSN HHTSRLRFPE IRFPRAAAKV
     VAKEGVAEMA VTELERENRG VLRVGLICGG PSAERGISLN SARSVLDHIQ GDDLLVSCYY
     IDPELNAYAI SSAQVYSNTP ADFDFKLKSL AHGFQSLTDF AEHLSASVDI VFPVIHGRFG
     EDGGIQELLE RHNIPFVGTG STECSHAFDK YNASLELDKL GFIKVPNFLI QAGSVSESEL
     SKWFLRNQID PSFGKVVVKP VRAGSSIGVT VAYGVADSLK KAEEIISQEI DDKVLVEVFL
     EGGSEFTAIV LDVGSGSVCH PVVLLPTEVE LQFHGWADAG EKDAIFNYRR KYLPTQQVTY
     HTPPRFAVDV IESIRKGASL LFKGLGLRDF ARIDGWFLPN SSRESSCSVG KFGRTESGTI
     VYTDINLISG MEQTSFLFQQ ASKVGFSHSN ILRSIIYHAC LRYPDLGSLD CMSGNLLRRS
     NSAQRSQAYS SHESIRKVFV IFGGDTSERQ VSLMSGTNVW LNLQVFDELE VTPCLLAPSN
     EQTSSLDLDK NQVDETSRTV WSLPYSLVLR HTTEEVLAAC IEAMEPTRAA LTSRLRELVM
     TDLKEGLKNH RWFAGFDIKD ELPVRYSLEQ WIKQAKEADA TVFIAVHGGI GEDGTLQSLL
     EAKGVPYTGP GAAASNICMD KVATSLALNH LSDMGVLTIK KDVRRKDDLL QIPILNVWHD
     LTRKLHCQSL CVKPARDGCS TGVARLCCAD DLAVYVKALE DCLVRIPSNS LSKAHGMIEM
     PKPPPELLIF EPFIETDEII VSSKSTNETK EQLLWEGQSR WVEITVGVVG TRGSMHSLSP
     SVTVKESGDI LSLEEKFQGG TGINLTPPPL MIIRNEALEK CKRHIELIAN TLQLEGFSRI
     DAFVNVDSGE VLVIEVNTVP GMTPSTVLIH QALAETPPVY PHQFFRRLLN LASERSP
//