ID A0A0B4E1E6_9RHOB Unreviewed; 653 AA.
AC A0A0B4E1E6;
DT 04-MAR-2015, integrated into UniProtKB/TrEMBL.
DT 04-MAR-2015, sequence version 1.
DT 27-MAR-2024, entry version 32.
DE SubName: Full=Dehydrogenase {ECO:0000313|EMBL:KID07024.1};
DE Flags: Fragment;
GN ORFNames=GC1_21125 {ECO:0000313|EMBL:KID07024.1};
OS Leisingera sp. ANG1.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Leisingera.
OX NCBI_TaxID=1002340 {ECO:0000313|EMBL:KID07024.1, ECO:0000313|Proteomes:UP000031201};
RN [1] {ECO:0000313|EMBL:KID07024.1, ECO:0000313|Proteomes:UP000031201}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ANG1 {ECO:0000313|EMBL:KID07024.1,
RC ECO:0000313|Proteomes:UP000031201};
RX PubMed=21551313; DOI=10.1128/JB.05139-11;
RA Collins A.J., Nyholm S.V.;
RT "Draft genome of Phaeobacter gallaeciensis ANG1, a dominant member of the
RT accessory nidamental gland of Euprymna scolopes.";
RL J. Bacteriol. 193:3397-3398(2011).
CC -!- SIMILARITY: Belongs to the GcvT family.
CC {ECO:0000256|ARBA:ARBA00008609}.
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:KID07024.1}.
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DR EMBL; AFCF02000016; KID07024.1; -; Genomic_DNA.
DR RefSeq; WP_039498875.1; NZ_AFCF02000016.1.
DR AlphaFoldDB; A0A0B4E1E6; -.
DR STRING; 1002340.GC1_21125; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000031201; Unassembled WGS sequence.
DR GO; GO:0016491; F:oxidoreductase activity; IEA:UniProtKB-KW.
DR Gene3D; 2.40.30.110; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.70.1400; Aminomethyltransferase beta-barrel domains; 1.
DR Gene3D; 3.30.9.10; D-Amino Acid Oxidase, subunit A, domain 2; 1.
DR Gene3D; 3.50.50.60; FAD/NAD(P)-binding domain; 1.
DR InterPro; IPR006076; FAD-dep_OxRdtase.
DR InterPro; IPR036188; FAD/NAD-bd_sf.
DR InterPro; IPR032503; FAO_M.
DR InterPro; IPR028896; GCST/YgfZ/DmdA.
DR InterPro; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR43757; AMINOMETHYLTRANSFERASE; 1.
DR PANTHER; PTHR43757:SF2; AMINOMETHYLTRANSFERASE, MITOCHONDRIAL; 1.
DR Pfam; PF01266; DAO; 1.
DR Pfam; PF16350; FAO_M; 1.
DR Pfam; PF01571; GCV_T; 1.
DR Pfam; PF08669; GCV_T_C; 1.
DR SUPFAM; SSF101790; Aminomethyltransferase beta-barrel domain; 1.
DR SUPFAM; SSF54373; FAD-linked reductases, C-terminal domain; 1.
DR SUPFAM; SSF51905; FAD/NAD(P)-binding domain; 1.
DR SUPFAM; SSF103025; Folate-binding domain; 1.
PE 3: Inferred from homology;
FT DOMAIN 2..212
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 215..268
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 272..539
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 568..645
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
FT NON_TER 1
FT /evidence="ECO:0000313|EMBL:KID07024.1"
SQ SEQUENCE 653 AA; 72165 MW; 5C93CC7263F30247 CRC64;
VTMAYAAGAR AMGAQIERFC PVIGTEQQPD GSWIVKTEKG DIHTQWVVNA GGLWGREVAA
MAGLTLPLQP TEHQYFVTES IDEVANLGRR LPSIADRDGE YYFRQEGNGF LIGAYEKDMR
FWAENGTPLD FAHELFPDDL DRIMENVIRA TERVPCAETA GVKRVINGPM IWSPDSNAIW
GPVPELKNYF CCTGIIPGFS QSGGLGLLAA QWMIEGEPQY DMFAWDLARF GDWADKKFTK
ARVEDQYAHR FAIHFPNEER SAGRPARVRP AYEMQKEMGC VFGLNCGWEH PLWFSGTPGT
TDTNSFTRQN WWEPVGREVK MLRENVGVID ISNFANYVIK GPGAFEWLDK LVANKVPTEV
GRSCLTPLIS VRGGVAGDFT ITKVADDEYM MVGSGMAERY HQRFFNMVEL PEGSTFEVAT
NRIAGFNVAG PKSRDMLQRM TNADLSNEAF RFMRSRTIDV AGVECLAIRV SFTGDLGWEL
HCAEEDQVKL YSALLAAAAE FDGGPVGGRA LGSLRIEKGY GSWGREYSQE YWPQEVGLAG
LIKLDKDFLN KDAYLKVKDN APREMLSAFE IDAVNDADAS GGEPVFTPDG KPVGRVTSGA
YGYSVGKSLA LGYANPAFAK PGDEVEVYIL GKPHKARILE AAAFDPSGAR LRA
//
