GenomeNet

Database: UniProt
Entry: A0A097AYK0_9VIBR
LinkDB: A0A097AYK0_9VIBR
Original site: A0A097AYK0_9VIBR 
ID   A0A097AYK0_9VIBR        Unreviewed;       126 AA.
AC   A0A097AYK0;
DT   07-JAN-2015, integrated into UniProtKB/TrEMBL.
DT   07-JAN-2015, sequence version 1.
DT   27-MAR-2024, entry version 55.
DE   RecName: Full=Glycine cleavage system H protein {ECO:0000256|HAMAP-Rule:MF_00272};
GN   Name=gcvH {ECO:0000256|HAMAP-Rule:MF_00272,
GN   ECO:0000313|EMBL:NOH38872.1};
GN   ORFNames=F0224_03000 {ECO:0000313|EMBL:NOI74631.1}, F0267_11545
GN   {ECO:0000313|EMBL:NOH38872.1}, TW71_11450
GN   {ECO:0000313|EMBL:KJY72780.1};
OS   Vibrio coralliilyticus.
OC   Bacteria; Pseudomonadota; Gammaproteobacteria; Vibrionales; Vibrionaceae;
OC   Vibrio.
OX   NCBI_TaxID=190893 {ECO:0000313|EMBL:NOH38872.1, ECO:0000313|Proteomes:UP000577246};
RN   [1] {ECO:0000313|EMBL:KJY72780.1}
RP   NUCLEOTIDE SEQUENCE.
RC   STRAIN=S2052 {ECO:0000313|EMBL:KJY72780.1};
RX   PubMed=25879706; DOI=10.1186/s12864-015-1365-z;
RA   Machado H., Sonnenschein E.C., Melchiorsen J., Gram L.;
RT   "Genome mining reveals unlocked bioactive potential of marine Gram-negative
RT   bacteria.";
RL   BMC Genomics 16:158-158(2015).
RN   [2] {ECO:0000313|Proteomes:UP000528382, ECO:0000313|Proteomes:UP000577246}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AIC-5 {ECO:0000313|EMBL:NOI74631.1,
RC   ECO:0000313|Proteomes:UP000528382}, and X00-12-4
RC   {ECO:0000313|EMBL:NOH38872.1, ECO:0000313|Proteomes:UP000577246};
RA   Kehlet-Delgado H., Mueller R.S.;
RT   "Draft genome sequencing and comparative genomics of hatchery-associated
RT   Vibrios.";
RL   Submitted (SEP-2019) to the EMBL/GenBank/DDBJ databases.
CC   -!- FUNCTION: The glycine cleavage system catalyzes the degradation of
CC       glycine. The H protein shuttles the methylamine group of glycine from
CC       the P protein to the T protein. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- COFACTOR:
CC       Name=(R)-lipoate; Xref=ChEBI:CHEBI:83088;
CC         Evidence={ECO:0000256|HAMAP-Rule:MF_00272};
CC       Note=Binds 1 lipoyl cofactor covalently. {ECO:0000256|HAMAP-
CC       Rule:MF_00272};
CC   -!- SUBUNIT: The glycine cleavage system is composed of four proteins: P,
CC       T, L and H. {ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- SIMILARITY: Belongs to the GcvH family. {ECO:0000256|ARBA:ARBA00009249,
CC       ECO:0000256|HAMAP-Rule:MF_00272}.
CC   -!- CAUTION: The sequence shown here is derived from an EMBL/GenBank/DDBJ
CC       whole genome shotgun (WGS) entry which is preliminary data.
CC       {ECO:0000313|EMBL:NOH38872.1}.
CC   ---------------------------------------------------------------------------
CC   Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC   Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC   ---------------------------------------------------------------------------
DR   EMBL; JXXR01000012; KJY72780.1; -; Genomic_DNA.
DR   EMBL; VTYS01000009; NOH38872.1; -; Genomic_DNA.
DR   EMBL; VTXB01000001; NOI74631.1; -; Genomic_DNA.
DR   RefSeq; WP_006961445.1; NZ_VTYS01000009.1.
DR   STRING; 190893.BA953_22910; -.
DR   GeneID; 66921581; -.
DR   KEGG; vct:JV59_21140; -.
DR   KEGG; vcy:IX92_17975; -.
DR   eggNOG; COG0509; Bacteria.
DR   OrthoDB; 9796712at2; -.
DR   Proteomes; UP000528382; Unassembled WGS sequence.
DR   Proteomes; UP000577246; Unassembled WGS sequence.
DR   GO; GO:0005960; C:glycine cleavage complex; IEA:InterPro.
DR   GO; GO:0019464; P:glycine decarboxylation via glycine cleavage system; IEA:UniProtKB-UniRule.
DR   CDD; cd06848; GCS_H; 1.
DR   Gene3D; 2.40.50.100; -; 1.
DR   HAMAP; MF_00272; GcvH; 1.
DR   InterPro; IPR000089; Biotin_lipoyl.
DR   InterPro; IPR002930; GCV_H.
DR   InterPro; IPR033753; GCV_H/Fam206.
DR   InterPro; IPR017453; GCV_H_sub.
DR   InterPro; IPR011053; Single_hybrid_motif.
DR   NCBIfam; TIGR00527; gcvH; 1.
DR   PANTHER; PTHR11715; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR   PANTHER; PTHR11715:SF41; GLYCINE CLEAVAGE SYSTEM H PROTEIN; 1.
DR   Pfam; PF01597; GCV_H; 1.
DR   SUPFAM; SSF51230; Single hybrid motif; 1.
DR   PROSITE; PS50968; BIOTINYL_LIPOYL; 1.
PE   3: Inferred from homology;
KW   Lipoyl {ECO:0000256|ARBA:ARBA00022823, ECO:0000256|HAMAP-Rule:MF_00272}.
FT   DOMAIN          21..103
FT                   /note="Lipoyl-binding"
FT                   /evidence="ECO:0000259|PROSITE:PS50968"
FT   MOD_RES         62
FT                   /note="N6-lipoyllysine"
FT                   /evidence="ECO:0000256|HAMAP-Rule:MF_00272,
FT                   ECO:0000256|PIRSR:PIRSR617453-50"
SQ   SEQUENCE   126 AA;  13906 MW;  15ED1DD4AA6DF252 CRC64;
     MDNTLKFADS HEWVRDNGDG TVTIGISEHA QEMLGDVVFV DLPEVEAEIE AGDSFSLVES
     VKAASDIYAP ITGEILEINE ELEDSPELIN EEPFEGGWIV KVKMSDASEL DNLKSAEEYL
     NSIEDE
//
DBGET integrated database retrieval system