Descriptions

The autoinhibited protein was predicted that may have potential autoinhibitory elements via cis-regPred.

Autoinhibitory domains (AIDs)

Target domain

Relief mechanism

Assay

cis-regPred

Accessory elements

No accessory elements

Autoinhibited structure

Activated structure

1 structures for Q0VR89

Entry ID Method Resolution Chain Position Source
AF-Q0VR89-F1 Predicted AlphaFoldDB

No variants for Q0VR89

Variant ID(s) Position Change Description Diseaes Association Provenance
No variants for Q0VR89

No associated diseases with Q0VR89

2 regional properties for Q0VR89

Type Name Position InterPro Accession
domain Cobalamin-independent methionine synthase MetE, C-terminal/archaeal 426 - 748 IPR002629
domain Cobalamin-independent methionine synthase MetE, N-terminal 5 - 312 IPR013215

Functions

Description
EC Number 2.1.1.14 Methyltransferases
Subcellular Localization
PANTHER Family
PANTHER Subfamily
PANTHER Protein Class
PANTHER Pathway Category No pathway information available

No GO annotations of cellular component

Name Definition
No GO annotations for cellular component

2 GO annotations of molecular function

Name Definition
5-methyltetrahydropteroyltriglutamate-homocysteine S-methyltransferase activity Catalysis of the reaction: 5-methyltetrahydropteroyltri-L-glutamate + L-homocysteine = L-methionine + tetrahydropteroyltri-L-glutamate.
zinc ion binding Binding to a zinc ion (Zn).

2 GO annotations of biological process

Name Definition
methionine biosynthetic process The chemical reactions and pathways resulting in the formation of methionine (2-amino-4-(methylthio)butanoic acid), a sulfur-containing, essential amino acid found in peptide linkage in proteins.
methylation The process in which a methyl group is covalently attached to a molecule.

No homologous proteins in AiPD

UniProt AC Gene Name Protein Name Species Evidence Code
No homologous proteins
10 20 30 40 50 60
MTTLHNLGFP RIGARRELKQ AQEAYWAGDL QQSELEHVGK SLRERHWALQ ADAGVDLMPV
70 80 90 100 110 120
GDFAWYDHIL EFSSLLGVVP SRFEQDANAP VNLDTLFRMA RGRAPTGTPA AACEMTKWFD
130 140 150 160 170 180
TNYHYLVPEL AADQTFRIAR ESLFEQVEEA KAQGHNPKPV IPGPLTYLYL SKGDRFEGAE
190 200 210 220 230 240
DSAKLALLDN LIPVYREILQ RFANQGVQWV QIDEPILVLD LPDSWQRAYL RVYDQLASAS
250 260 270 280 290 300
QTKLLLATYF GGLGNNLFTA LELPVHGLHL DRVRGNDDLG QVIPRLGDKV LSLGVINGRN
310 320 330 340 350 360
IWRTDLDAAL DNITALHNEL GDRLWLAPSC SLLHCPVDLE QEDTLDNELK SWLSFAKQKL
370 380 390 400 410 420
EELALLGGAL RGNSNVNSGL QTQRAALQAR GLSSRIHNPA VAQRLADASQ LSRDRVSPFA
430 440 450 460 470 480
ERIAQQQHAL QLPAFPTTTI GSFPQTREIR TARRDWKAGK LNDAQYQQQM QEEIARCIRY
490 500 510 520 530 540
QEEVELDVLV HGEAERNDMV EYFGELLDGF AFTRFGWVQS YGSRCVKPPI IFGDVQRPQA
550 560 570 580 590 600
MTVEWARYAQ SLTHKPVKGM LTGPVTILQW SFVRDDQPRA DTCRQIALAL RDEVQDLEKA
610 620 630 640 650 660
GIKVIQIDEP ALREGLPLRQ EEWTQYLDWA VDCFRLATVS VDDDTQIHTH MCYSEFNDII
670 680 690 700 710 720
EAIAALDADV ITIETSRSNM ELLDAFRDFH YPNDIGPGVY DIHSPNEPDV AWMVQLMEKA
730 740 750 760
AERLPKERLW VNPDCGLKTR KWDETRAALA NMVNAAKQLR QAS