ID A3SNQ9_ROSNI Unreviewed; 801 AA.
AC A3SNQ9;
DT 03-APR-2007, integrated into UniProtKB/TrEMBL.
DT 03-APR-2007, sequence version 1.
DT 27-MAR-2024, entry version 66.
DE RecName: Full=Dehydrogenase {ECO:0008006|Google:ProtNLM};
GN ORFNames=ISM_14575 {ECO:0000313|EMBL:EAP76099.1};
OS Roseovarius nubinhibens (strain ATCC BAA-591 / DSM 15170 / ISM).
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Roseovarius.
OX NCBI_TaxID=89187 {ECO:0000313|EMBL:EAP76099.1, ECO:0000313|Proteomes:UP000005954};
RN [1] {ECO:0000313|EMBL:EAP76099.1, ECO:0000313|Proteomes:UP000005954}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=ATCC BAA-591 / DSM 15170 / ISM
RC {ECO:0000313|Proteomes:UP000005954};
RA Moran M.A., Ferriera S., Johnson J., Kravitz S., Halpern A., Remington K.,
RA Beeson K., Tran B., Rogers Y.-H., Friedman R., Venter J.C.;
RL Submitted (DEC-2005) to the EMBL/GenBank/DDBJ databases.
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:EAP76099.1}.
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DR EMBL; AALY01000002; EAP76099.1; -; Genomic_DNA.
DR AlphaFoldDB; A3SNQ9; -.
DR STRING; 89187.ISM_14575; -.
DR eggNOG; COG0404; Bacteria.
DR eggNOG; COG0665; Bacteria.
DR HOGENOM; CLU_007884_11_1_5; -.
DR Proteomes; UP000005954; 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;
KW Reference proteome {ECO:0000313|Proteomes:UP000005954}.
FT DOMAIN 2..356
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 359..413
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 417..684
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 725..793
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 801 AA; 88760 MW; 5412161F3838899A CRC64;
MIGGGVIGCS ILYHLTKLGW TDVMLLERDE LTSGSTWHAA ANIHGLHDSA NISRLQHYTM
TLYNELEAET GQSCGVFQPG SLYLAQTEAR EHQLRLQAAK AKLYGMNFHE VSRDEAERLH
PLVNFDGIRC IMWEPDGGNV DPSGVTNAYA VGARQRGAEI HRFTPVTGTD QQPDGSWIVR
TPKGDIHTEW VINAAGLWGR EVAALAGIEV PLQPTEHQYF VTETIAEIDA MDRRLPSVAD
RDGEYYLRQE GKGLLIGAYE KDMRFWAENG TPLDFAHDLF ADDLDRIMEN VMRAMDRVPV
AAEAGVKRVI NGPMIWSPDS NVILGPVPEL KNYFMCGGII PGFSQSAGMG LMCAQWMIEG
EMKYDMFPWD VARFGLWAND RKFVKAKVED VYSHRFAIHY PNEERAAGRP LRTRPAYEMQ
KDMGAVFGLN YGWEHPQWFA GEKGAKDTNG FTRQNWWEPV GEECRMLRER AGIIDISNFA
KYRCKGPGAE DWLNSVFANK MPKSVGRSCL TPLISVRGGI AGDATVTRTA EDEFWIVSSG
MAERYHKRFF DMVPLPEGTT FESHTEAMCG FNVAGPKSRD MLQRLTNASL ATEDFPFMRS
KVIELGGVEC LALRVSFTGD LGWELHCKTE DQAKLYAALL EAGKEFGAGP VGARALMSMR
VEKGYGSWSR EYSPEYYPHE VGLAALCKMD KDFLHKAAAE KALAEPEREQ LVLIHVDEAA
VTASNADATG GEPIFRDGKG IGRVTSGTYG YSVGMSLALG YVKAGTAAPG DAVDVMILGQ
PHKAVILHEP PFDPEGKRLR A
//