ID A0A017HPL5_9RHOB Unreviewed; 806 AA.
AC A0A017HPL5;
DT 11-JUN-2014, integrated into UniProtKB/TrEMBL.
DT 11-JUN-2014, sequence version 1.
DT 27-MAR-2024, entry version 33.
DE SubName: Full=Sarcosine dehydrogenase {ECO:0000313|EMBL:EYD76068.1};
DE EC=1.5.8.3 {ECO:0000313|EMBL:EYD76068.1};
GN ORFNames=Rumeso_02375 {ECO:0000313|EMBL:EYD76068.1};
OS Rubellimicrobium mesophilum DSM 19309.
OC Bacteria; Pseudomonadota; Alphaproteobacteria; Rhodobacterales;
OC Roseobacteraceae; Rubellimicrobium.
OX NCBI_TaxID=442562 {ECO:0000313|EMBL:EYD76068.1, ECO:0000313|Proteomes:UP000019666};
RN [1] {ECO:0000313|EMBL:EYD76068.1, ECO:0000313|Proteomes:UP000019666}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=DSM 19309 {ECO:0000313|EMBL:EYD76068.1,
RC ECO:0000313|Proteomes:UP000019666};
RA Fiebig A., Goeker M., Klenk H.-P.P.;
RL Submitted (FEB-2013) 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:EYD76068.1}.
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DR EMBL; AOSK01000061; EYD76068.1; -; Genomic_DNA.
DR RefSeq; WP_037282960.1; NZ_KK088613.1.
DR AlphaFoldDB; A0A017HPL5; -.
DR STRING; 442562.Rumeso_02375; -.
DR PATRIC; fig|442562.3.peg.2343; -.
DR HOGENOM; CLU_007884_11_0_5; -.
DR OrthoDB; 7156675at2; -.
DR Proteomes; UP000019666; Unassembled WGS sequence.
DR GO; GO:0008480; F:sarcosine dehydrogenase activity; IEA:UniProtKB-EC.
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; IPR013977; GCV_T_C.
DR InterPro; IPR006222; GCV_T_N.
DR InterPro; IPR029043; GcvT/YgfZ_C.
DR InterPro; IPR027266; TrmE/GcvT_dom1.
DR PANTHER; PTHR13847:SF193; PYRUVATE DEHYDROGENASE PHOSPHATASE REGULATORY SUBUNIT, MITOCHONDRIAL; 1.
DR PANTHER; PTHR13847; SARCOSINE DEHYDROGENASE-RELATED; 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 Oxidoreductase {ECO:0000313|EMBL:EYD76068.1};
KW Reference proteome {ECO:0000313|Proteomes:UP000019666}.
FT DOMAIN 8..362
FT /note="FAD dependent oxidoreductase"
FT /evidence="ECO:0000259|Pfam:PF01266"
FT DOMAIN 367..420
FT /note="FAD dependent oxidoreductase central"
FT /evidence="ECO:0000259|Pfam:PF16350"
FT DOMAIN 422..689
FT /note="Aminomethyltransferase folate-binding"
FT /evidence="ECO:0000259|Pfam:PF01571"
FT DOMAIN 714..798
FT /note="Glycine cleavage T-protein C-terminal barrel"
FT /evidence="ECO:0000259|Pfam:PF08669"
SQ SEQUENCE 806 AA; 88036 MW; 9E33210CA914D41F CRC64;
MIPTHAQVVV IGGGIVGCST AYHLARDHGA EVVLLEQGKL TSGSTWHAAG LVGQLRSSAG
VTRLLKHSVE LYKRLDEETG LATGWKMTGC LRLATNPDRW TEYRRLATTA RSFGMEMELI
PPREVKEMWP LLEVDDLVGA SWLPTDGQAN PADIAASLAK GARMAGAKIV EGIRVTGFDM
DEGRIHTVQT TLGPIHCEKV VNCAGMWARD VGAMAGAVVP LQPVRHQYIV TEAIPDLAPN
APTLRDPDRR TYFKEEVGGL VMGGYEPDPQ PLGTGEVPFQ EFHLYDDDWD HFAPHMEQAI
ERIPALAETG VKRMINGAES FTPDGNFILG RPPHLKNFYV GAGFNAFGIA SGGGAGWALA
SWVMEDEAPM DLWPVDIRRF GSIHADRDWV LQRTCEAYGK HYTIAWPHEE YESGRPRLTS
PLYQRLLGAG AVMGSKLGWE RANWFADEPG AEDEPSMNRP AWADAVAREH RHTRTHASVF
DQTSFAKFEL SGPGAAEALD ALCAGDVLKA PGRLTYTQLL NSRGGIEADL TVARLGPEHF
YIVTGTGFRT HDGAWIDDHL PSGLRLRDVT EEWGVLALMG PRARDILRAV TEANVENDAF
PFAHWREVAI AGQPVRALRI TYVGELGWEL HVPLHGLAAV YDALMEADPD LRPAGYRAIE
SLRLEKGYRA WSSDITPNDT PLEAGLGWAT KLRTPRHFLG REALERQARG PLTKRLLGFR
LADLDAVLLG RETILRDGEP AGYLTSGGFG PTVGAPIGYG YVRDPGGLTD EALLGSSYAV
VVAGETVPAR PSLRPFHDPE NAATRI
//
